Three-dimensional model of a complex between a Fc epsilon receptor alpha chain and a Fc region of an IgE antibody and uses thereof

ABSTRACT

The present invention includes three-dimensional models of complexes between antibody receptor proteins, such as FcεRIα proteins, and antibodies, such as Fc-Cε3/Cε4 regions of IgE antibodies, as well as methods to produce such models. The present invention also includes muteins having increased stability and/or antibody binding activity, as well as methods to produce such muteins, preferably using information derived from three-dimensional models of the present invention. Also included are nucleic acid sequences encoding muteins of the present invention and use of those sequences to produce such muteins. Also included is the use of the model to identify compounds that inhibit the binding of an antibody receptor protein to an antibody. The present invention also includes uses of such muteins and inhibitory compounds, for example, in methods to diagnose and protect animals from allergy and other abnormal immune responses.

CROSS-REFERENCE TO RELATED APPLICATION

[0001] This Application claims priority to provisional application U.S. Serial No. 60/189,853, filed Mar. 15, 2000, “THREE-DIMENSIONAL MODEL OF A COMPLEX BETWEEN A Fe EPSILON RECEPTOR ALPHA CHAIN AND A Fe REGION OF AN IgE ANTIBODY AND USES THEREOF.”

[0002] This invention was made at least in part with government support under NIH Grant No. RO1 A138972, awarded by the National Institutes of Health to Northwestern University. The government has certain rights to this invention.

FIELD OF THE INVENTION

[0003] The present invention relates to a crystal and a three-dimensional (3-D) model of a complex between a Fe epsilon receptor alpha chain (FcεRIα, or FceRIa) protein and a constant region of an IgE antibody that includes the Cε3 and Cε4 domains (Fc-Cε3/Cε4, or Fc-Cε3/Cε4, region). The present invention also relates to the use of that model to produce muteins and inhibitors useful in the diagnosis and treatment of allergy and the regulation of other immune responses in an animal.

BACKGROUND OF THE INVENTION

[0004] Antibody Fc-receptors (FcRs) play an important role in the immune response by coupling the specificity of secreted antibodies to a variety of cells of the immune system. A number of cell types, including macrophages, mast cells, eosinophils, and basophils, express membrane-bound FcRs at their surfaces. The binding of antibodies to FcRs provides antigen-specificity to these cells, which upon activation release further cell-specific mediators of the immune response, such as interleukins, initiators of inflammation, leukotrienes, prostaglandins, histamines, or cytotoxic proteins. The adoptive specificity of the FcRs allows a combinatorial approach to pathogen elimination, by coupling the diversity of antibody antigen-recognition sites to the variety of cell-types expressing these receptors.

[0005] FcR-initiated mechanisms are important in normal immunity to infectious disease as well as in allergies, antibody-mediated tumor recognition, autoimmune diseases, and other diseases in which immune responses are abnormal (i.e., not regulated). Recent experiments with transgenic mice have demonstrated that the FcRs control key steps in the immune response, including antibody-directed cellular cytotoxicity and inflammatory cascades associated with the formation of immune complexes; see, for example, Ravetch et al., 1998, Annu Rev Immunolo 16, 421-432. Receptors that bind IgG (FcgRI, FcgRII, and FcgRIII, known collectively as FcgRs) mediate a variety of inflammatory reactions, regulate B-cell activation, and also trigger hypersensitivity reactions. The high affinity Fc epsilon receptor (also known as the IgE receptor or FceRI) is associated with the activation of mast cells and the triggering of allergic reactions and anaphylactic shock. Knockout mice for the FceRI alpha chain (FcεRIα) are unable to mount IgE-mediated anaphylaxis (see for example, Dombrowicz et al., 1993, Cell 75, 969-976), although FcgRs are still able to activate mast cells (see, for example, Dombrowicz et al., 1997, J. Clin. Invest. 99, 915-925; Oettgen et al., 1994, Nature 370, 367-370). FceRI has also been shown to trigger anti-parasitic reactions from platelets and eosinophils as well as deliver antigen into the MHC class II presentation pathway for the activation of T cells; see, for example, Gounni et al., 1994, Nature 367, 183-186; Joseph et al., 1997, Eur. J. Immunol. 27, 2212-2218; Maurer et al., 1998, J. Immunol. 161, 2731-2739. The beta subunit of FceRI has been associated with asthma in genetic studies; see, for example, Hill et al., 1996, Hum. Mol. Genet. 5, 959-962; Hill et al., 1995, Bmj 311, 776-779; Kim et al., 1998, Curr. Opin. Pulm. Med. 4, 46-48; Mao et al., 1998, Clin. Genet. 53, 54-56; Shirakawa et al., 1994, Nat. Genet. 7, 125-129. A significant fraction of the population (˜20%) may be affected by allergies, and this century has seen a substantial increase in asthma. Since IgE binding to FceRI is a requisite event in the reaction to different allergens, therapeutic strategies aimed at inhibiting FceRI could provide a useful treatment for these diseases. For example, monoclonal antibodies that target IgE and block receptor binding have shown therapeutic potential; see, for example, Heusser et al., 1997, Curr. Opin. Immunol. 9, 805-813.

[0006] FceRI is found as a tetrameric (abg₂) or trimeric (ag₂) membrane bound receptor on the surface of mast cells, basophils, eosinophils, langerhans cells and platelets. The alpha chain, also referred to as FcεRIα, of FceRI binds IgE molecules with high affinity (K_(D) of about 10⁻⁹ to 10⁻¹⁰ moles/liter (M)), and can be secreted as a 172-amino acid soluble, IgE-binding fragment by the introduction of a stop codon before the single C-terminal transmembrane anchor; see, for example, Blank et al., 1991, E. J. Biol. Chem. 266, 2639-2646, which describes the secretion of a soluble IgE-binding fragment of 172 amino acids. The extracellular domains of the human FcεRIα protein belong to the immunoglobulin (Ig) superfamily and contain seven N-linked glycosylation sites. Glycosylation of FcεRIα affects the secretion and stability of the receptor, but is not required for IgE-binding; see, for example, LaCroix et al., 1993, Mol. Immunol. 30, 321-330; Letourneur et al., 1995, J. Biol. Chem. 270, 8249-8256; Robertson, 1993, J. Biol. Chem. 268, 12736-12743; Scarselli et al., 1993, FEBS Lett 329, 223-226. The beta and gamma chains of FceRI are signal transduction modules.

[0007] Prior investigators have disclosed the nucleic acid sequence for human FcεRIα; see, for example, U.S. Pat. No. 4,962,035, by Leder, issued Oct. 9, 1990; U.S. Pat. No. 5,639,660, by Kinet et al., issued Jun. 17, 1997; Kochan et al., 1988, Nucleic Acids Res. 16, 3584; Shimizu et al., 1988, Proc. Natl. Acad. Sci. USA 85, 1907-1911; and Pang et al., 1993, J. Immunol. 151, 6166-6174. Nucleic acid sequences have also been reported for the human FceRI beta and gamma chains; see, respectively, Kuster et al., 1992, J. Biol. Chem. 267, 12782-12787; Kuster et al., 1990, J. Biol. Chem. 265, 6448-6452. Nucleic acid sequences have also been reported for nucleic acid molecules encoding canine FcεRIα, murine FcεRIα, rat FcεRIα, feline FcεRIα and equine FcεRIα proteins; see, respectively, GenBank™ accession number D16413; Swiss-Prot accession number P20489 (represents encoded protein sequence); GenBank accession number J03606; PCT Publication No. WO 98/27208, by Frank et al., published Jun. 25, 1998, referred to herein as WO 98/27208; and PCT Publication No. WO 99/38974, by Weber et al., published Aug. 5, 1999, referred to herein as WO 99/38974. In addition, methods to detect IgE antibodies using a FcεRIα protein have been reported in PCT Publication No. WO 98/23964, by Frank et al., published Jun. 4, 1998, referred to herein as WO 98/23964; WO 98/27208, ibid.; PCT Publication No. WO 98/45707, by Frank et al., published Oct. 15, 1998, referred to herein as WO 98/45707; and WO 99/38974, ibid. WO 98/23964, WO 98/27208, WO 98/45707 and WO 99/38974 are each incorporated by reference herein in its entirety.

[0008] There have been several reports of the use of mutagenesis and swapping techniques to attempt to identify amino acids of either FcεRIα or IgE involved in the binding of (i.e., interaction between) those respective proteins, reports attempting to model FcεRIα proteins based on homology to other Ig-superfamily members, and reports that identify compounds that apparently inhibit such binding; see, for example, Cook et al., 1997, Biochemistry 36, 15579-15588; Hulett et al., 1994, J. Biol. Chem. 269, 15287-15293; Hulett et al., 1995, J. Biol. Chem 270, 21188-21194; Mallamaci et al., 1993, J. Biol. Chem. 268, 22076-22083; Robertson, 1993, ibid.; Scarselli et al., 1993, ibid. McDonnell et al., 1997, Biochem. Soc. Trans. 25, 387-392; McDonnell et al., 1996, Nat. Struc. Biol. 3, 419-426; PCT Publication No. WO 97/40033, by Cheng et al., published Oct. 30, 1997; U.S. Pat. No. 5,180,805, by Gould et al, issued Jan. 19, 1993; U.S. Pat. No. 5,693,758, by Gould et al., issued Dec. 2, 1997; PCT Publication No. WO 96/01643, by Gould et al., published Jan. 25, 1996; PCT Publication No. WO 95/14779, by Gould et al., published Jun. 1, 1995. None of these references, however, describe isolated crystals of FcεRIα proteins or 3-D models derived from crystals.

[0009] Despite what is known about FcRs and their interaction with antibodies, there remains a need for FcRs and antibodies with improved characteristics, such as enhanced affinity for their ligands, altered substrate specificity, increased stability, and increased solubility for use in diagnosis, treatment and prevention of allergy and other abnormal immune responses. Also needed for safe and efficacious compounds to prevent or treat allergy and to regulate other immune responses in an animal.

SUMMARY OF THE INVENTION

[0010] The present invention includes isolated crystals of a complex between the extracellular domains of antibody receptor proteins (FcRs) and constant regions (Fc regions) of antibodies, three-dimensional (3-D) models of such crystals and modifications of such models. The present invention also includes compounds that inhibit the ability of FcRs to bind to antibodies as well as FcR muteins and other modified FcRs as well as antibody muteins and other modified antibodies. Also included in the present invention are methods to produce and use such crystals, models, inhibitory compounds, muteins, and other modified proteins. As such, the present invention includes FcRs and antibodies with improved functions such as increased stability, increased affinity for an Fc domain of an antibody, altered substrate specificity, and increased solubility, including but not limited to reduced aggregation. Such proteins, also referred to as muteins, are useful to detect allergy and other immune response abnormalities as well as to protect an animal from such abnormalities. The present invention also provides safe and efficacious inhibitory compounds to protect (e.g., prevent, treat, reduce the consequences of) an animal from allergy and to regulate other immune responses in an animal.

[0011] The present invention includes a 3-D model of a complex between an extracellular domain of a human high affinity Fc epsilon receptor alpha chain (FcεRIα) protein and a human IgE Fc region comprising Cε3 and Cε4 domains, wherein the model substantially represents the atomic coordinates specified in Table 1. The present invention also includes a 3-D model comprising a modification of a model substantially representing the atomic coordinates specified in Table 1. Also included in the present invention are methods to produce such models.

[0012] The present invention also includes an isolated crystal of a complex between an extracellular domain of a human high affinity Fc epsilon receptor alpha chain protein and a human IgE Fc region comprising Cε3 and Cε4 domains.

[0013] The present invention includes a method to identify a compound that inhibits the binding between an IgE antibody and a FcεRIα protein. The method includes the step of using a 3-D model of the present invention, and particularly one substantially represents the atomic coordinates specified in Table 1. Also included in the present invention are inhibitory compounds identified using such a method. Also included are therapeutic compositions that include such inhibitory compounds and methods to use such therapeutic compositions to protect an animal from allergy or to regulate other immune responses (e.g., protect an animal from other abnormal immune responses).

[0014] The present invention also includes a mutein that binds to a Fc domain of an antibody or to a Fc binding domain of a FcR. Such a mutein has an improved function compared to a protein that includes SEQ ID NO:2 or SEQ ID NO:6, respectively. Examples of such an improved function include increased stability, increased affinity for an Fc domain of an antibody, altered substrate specificity, decreased aggregation, and increased solubility. Such a mutein is produced by a method that includes the following steps: (a) analyzing a 3-D model substantially representing the atomic coordinates specified in Table 1 to identify at least one amino acid of the protein represented by the model which if replaced by a specified amino acid would effect an improved function of the protein; and (b) replacing the identified amino acid(s) to produce the mutein having such an improved function. The present invention also includes a mutein having an improved function compared to an unmodified FcεRIα protein or IgE Fc region.

[0015] Also included are muteins that are chemically modified FcεRIα proteins or antibodies. Also included are nucleic acid molecules that encode muteins of the present invention, recombinant molecules and recombinant cells including such nucleic acid molecules and methods to produce such muteins. Also included are diagnostic reagents and diagnostic kits including such muteins, therapeutic compositions including such muteins, and methods to detect or protect an animal from allergy or other abnormal immune responses.

[0016] The present invention also includes a method to improve a function of a FcεRIα protein or IgE Fc region which includes the steps of: (a) analyzing a 3-D model substantially representing the atomic coordinates specified in Table 1 to identify at least one amino acid of the protein which if replaced by a specified amino acid improves at least one of the functions of the protein; and (b) replacing the identified amino acid(s) to produce a mutein having at least one of the improved functions.

BRIEF DESCRIPTION OF THE DRAWINGS

[0017]FIG. 1 shows an electron density map and ribbon diagrams depicting the overall structure of the IgE-Fc:FcεRIα complex. FIG. 1 a shows a stereo diagram from a σ_(a)-weighted 2F_(o)-F_(c) simulated annealing omit electron density map at 3.5 angstroms. The complex is contoured at 1.25σ. FcεRIα residues 129-136 of FcεRIα and IgE-Fc loop residues 334-336 and 362-364 are shown. FIG. 1b is a side view of the IgE-Fc:FcεRIα complex depicting the two Fc chains (yellow and red ribbon, upper left of figure) and the FcεRIα chain (blue ribbon, lower right of figure). Binding sites 1 and 2 are indicated. The cell membrane would lie below the receptor. FIG. 1c is a top view of the IgE-Fc:FcεRIα complex shown in FIG. 1b.

[0018]FIG. 2 shows a surface representation of the IgE-Fc:FcεRIα complex. FIG. 2a is a side view of the IgE-Fc:FcεRIα complex highlighting how the convex surface of the receptor interacts asymmetrically with the two IgE-Fc Cε3 domains. The two Fc chains are in yellow and red while the FcεRIα chain is in blue. Carbohydrate surfaces are white, detergent surface is black. FIG. 2b is a top view of the IgE-Fc:FcεRIα complex surface representation shown in FIG. 2a. FIG. 2c is a superposition of the two IgE-Fc Cε3 domains. The twofold symmetry of the IgE-Fc domains is broken in the Cε2-Cε3 linker region (residues 328-336) by interactions with the receptor. Superposition of the Cε3 domains leads to a small displacement in the Cε4 domain, because of a 3° difference in Cε3 and Cε4 pseudo-dyad axes. FIG. 2d is a surface representation of both IgE-Fc and FcεRIα in which the IgE-Fc:FcεRIα complex has been separated to expose the surfaces involved in binding. The IgE (upper left) is oriented to give an end-on view of the Cε3 domains. Binding residues that bind FcεRIα are shown in yellow (Site 1) and red (Site 2). A top and side view of the FcεRIα is shown on the right-hand side of FIG. 2d. Residue Y131 of site 1 and the binding pocket for P426 of the IgE-Fc are labeled. Carbohydrate is shown in grey.

[0019]FIG. 3 details the interactions in the IgE-Fc:FcεRIα complex at Site 1 and Site 2. FIG. 3a is a plot showing the buried surface area of residues in the IgE-Fcε3 domains. The top half of the graph shows residues buried in the Site 1 interaction (yellow bars), while the bottom half of the graph shows residues buried in the Site 2 interaction (red bars). The IgE loops are identified above the plot. 50 Å of buried surface area of N394 is due to attached carbohydrate. FIG. 3b is a stick model diagram of residue interactions at Site 1. The IgE-Fc and FcIa chains are tan and blue, respectively. Binding loops are labeled at their termini, side chains of residues buried in the complex are shown and Y131 is labeled. FIG. 3c is a stick model diagram of the residue interactions at Site 2. The IgE-Fc and FcεRIα chains are red and blue, respectively. Side chains of residues buried in the complex are shown. FIG. 3d is a space filling model showing binding of CHAPS detergent molecule in the IgE-Fc:FcεRIα complex. Atoms less than 4A apart have dotted lines between them and the residues are labeled. No density appears for the flexible top-end of the detergent and those atoms are not labeled.

[0020]FIG. 4 illustrates the conservation of amino-acid residues and contacts at the IgE-Fc:FcεRIα interfaces in IgG receptors and antibodies. Contacting residues are defines as interatomic distances <4 Å. FIG. 4a shows the Site 1 interacting residues and their conservation in related human receptors and antibodies. Absolutely conserved residues are highlighted in bold and partially conserved residues are lightly highlighted (yellow for IgE, blue for FcεRIα). Dark lines are drawn for residues making the largest number of contacts across the interface, lighter lines for intermediate number of contacts, and dashed lines for the fewest contacts. FIG. 4b shows the Site 2 interacting residues and their conservation in human related Fc receptors and antibodies. Receptor residues are highlighted in blue, antibody residues in red. Three residues in IgG2 (PVA) that disrupt binding to FcγRI are boxed in black. FIG. 4c is a closeup of the Site 2 trp/proline interaction (FcR surface with IgE-ribbon interaction). Also shown are residues implicated in the IgG specificity between different receptor subtypes (corresponding to residues 332-334 in IgE) that interact with the FG loop. FIG. 4d is shows how FcRY131 in Site 1 interacts with a shallow pocket on the Cε3 domain that could be a source of specificity for IgG interactions (Y changes to H or R in FcγRII and FcγRIII).

[0021]FIG. 5 depicts a kinetic scheme for the binding of IgE to its receptor. The interaction of each Cε3 domain with distinct surfaces of the FcεRIα structure suggests a kinetic scheme in which transient release of one of the Cε3 domains may occur within the complex. This could lead to two distinct pathways for the association and dissociation of the complex, consistent with the experimental observation of two distinct off-rates. Transient opening of the complex may allow inhibitors to enhance the dissociation of receptor-bound IgE by preventing the re-binding of an exposed Cε3 domain within the complex.

[0022]FIG. 6 is a ribbon-model showing the superposition of the Fc portion of an intact IgG antibody (1IGY)27 and IgG Fc receptor FcγRII22 onto the IgE-Fc:FcεRIα complex. The IgE complex is shown in beige and the IgG homologues in blue. Only a minor adjustment of the other IgG domain is required to fit the IgE complex.

[0023]FIG. 7 shows a hypothetical model for an intact IgE:Fc receptor complex. The Fc chains are in red and yellow, the FcεRIα chain is in blue. Antibody Fab regions are shown in beige.

DETAILED DESCRIPTION OF THE INVENTION

[0024] The present invention includes isolated crystals of complexes between the extracellular domains of FcRs and Fc regions of antibodies, 3-D models of such crystals and modifications of such models. The present invention also includes compounds that inhibit the ability of FcRs to bind to antibodies as well as muteins and other modified FcRs and antibodies. Also included in the present invention are methods to produce and use such crystals, models, inhibitory compounds, muteins, and other modified proteins.

[0025] The present invention includes an isolated crystal of a complex between an extracellular domain of a high affinity Fc epsilon receptor alpha chain (FcεRIα) and a Fc region comprising the Cε3 and Cε4 domains of an IgE antibody (Fc-Cε3/Cε4), a 3-D model of such a crystal and a modification of such a model. As used herein, the term “a” entity or “an” entity refers to one or more of that entity; for example, a crystal or a model refers to one or more crystals or models, respectively. As such, the terms “a” (or “an”), “one or more” and “at least one” can be used interchangeably herein. It is also to be noted that the terms “comprising”, “including”, and “having” can be used interchangeably. Furthermore, a compound “selected from the group consisting of” refers to one or more of the compounds in the list that follows, including mixtures, or combinations, of two or more of the compounds.

[0026] As used herein, an extracellular domain of a FcεRIα protein is the portion of the FceRI alpha chain that is exposed to the environment outside the cell and that binds to the Fc domain of an IgE antibody. Such an extracellular domain can be (a) a complete extracellular domain which is a domain that extends from the first amino acid of a mature FceRI alpha chain through the last amino acid prior to the start of the transmembrane region or a domain that is functionally equivalent, in that such a domain includes a D1 and D2 domain, displays a similar affinity for the IgE antibody to which such an FcεRIα protein naturally binds, and produces crystals having sufficient quality to enable structure determination, or (b) a fragment of any of the extracellular domains of (a), wherein the fragment retains its ability to bind to the Fc domain of an antibody. As used herein, the terms binding to an antibody and binding to the Fc domain (i.e., constant region) of an antibody can be used interchangeably since it is recognized that a FcR binds to the Fc domain of an antibody. A FcR (i.e., a protein that can bind to an antibody), such as a FcεRIα protein, can be a full-length FcR (e.g., a full-length FceRI alpha chain), or any fragment thereof, wherein the fragment binds to an antibody. Similarly an antibody, or an Fc region thereof, can be a full-length antibody, or full-length Fc region thereof, or any fragment thereof that binds to a FcR. In one embodiment an Fc region comprises Cε3 and Cε4 domains. Preferably a FcR binds to an antibody with an affinity (K_(A)) of at least about 10⁸ liters/mole (M⁻¹), more preferably of at least about 10⁹ M⁻¹, and even more preferably of at least about 10¹⁰ M⁻¹.

[0027] The present invention is surprising in several aspects. For example, this is the first report of an isolated crystal of a complex between an extracellular domain of a FcεRIα protein and a Fc-Cε3/Cε4 region of an IgE antibody, and in particular of an isolated crystal of sufficient quality that a crystal structure, i.e., a 3-D model, could be derived therefrom. Generation of such a crystal was very difficult and non-obvious and has been attempted by others without success. The inventors tried many approaches before discovering a preferred FcεRIα protein and a preferred Fc-Cε3/Cε4 region from which to make a useful crystal. Part of the reason for the difficulty is that the FcεRIα protein is highly glycosylated. Although crystals could be produced using a FcεRIα protein that consists of amino acids 1 through 176 of the mature human FcεRIα protein, a protein that is denoted herein as PhFcεRIα₁₋₁₇₆, or the hFcεRIα₁₋₁₇₆ protein, and has an amino acid sequence denoted herein as SEQ ID NO:2, much better crystals could be generated using a FcεRIα protein that consists of amino acids 1 through 176 of the mature human FcεRIα protein that had been mutated to replace four N-linked glycosylation sites with other amino acids at positions 74, 135, 142 and 143 of SEQ ID NO:2 to produce a protein having SEQ ID NO:4, the protein being denoted herein as PhFcεRIα_(1-176mut), or the hFcεRIα_(1-176mut) protein. An example of a nucleic acid molecule encoding PhFcεRIα₁₋₁₇₆ is referred to herein as nhFcεRIα₁₋₅₂₈, the nucleic acid sequence of which is denoted herein as SEQ ID NO:1. An example of a nucleic acid molecule encoding PhFcεRIα_(1-176mut) is referred to herein as nhFcεRIα_(1-528mut), the nucleic acid sequence of which is denoted herein as SEQ ID NO:3. Identification of an appropriate Fc-Cε3/Cε4 region to crystallize was also difficult. The first such region to be used successfully is referred to herein as PhFc-Cε3/Cε4₁₋₂₂₂ which is composed of the four amino acids alanine, aspartic acid, proline and cysteine at the amino terminus followed by amino acids 330 through 547 of the human IgE Fc constant region, using the numbering system of Dorrington et al, 1978, Immunol Rev 41, 3-25. PhFc-Cε3/Cε4₁₋₂₂₂ is represented herein by SEQ ID NO:6. An example of a nucleic acid molecule encoding PhFc-Cε3/Cε4₁₋₂₂₂ is referred to herein as nhFc-Cε3/Cε4₁₋₆₆₆, the nucleic acid sequence of which is referred to herein as SEQ ID NO:5. It was also discovered that better crystals are generated when PhFcεRIα₁₋₁₇₆ and PhFc-Cε3/Cε4₁₋₂₂₂ are produced in insect cells, using a method such as that described in the Examples.

[0028] Determination of the crystal structure of the complex between PhFcεRIα_(1-176mut) and PhFc-Cε3/Cε4₁₋₂₂₂, each produced in Trichoplusia ni (Hi-5) cells, resulted in a 3-D model that substantially represents the atomic coordinates specified in Table 1. Amino acids are represented herein by their standard three or one letter codes; see, for example, Sambrook et al., Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Labs Press, 1989, which is incorporated herein by reference in its entirety. Prior to obtaining a crystal of sufficient quality to solve its crystal structure using insect-cell produced PhFcεRIα_(1-176mut) and PhFc-Cε3/Cε4₁₋₂₂₂, a number of other proteins were tried without success, as described in the Examples. , including a FcεRIα protein spanning from amino acid 1 through 171 of SEQ ID NO:2 produced in Pichia pastoris, and FcεRIα proteins spanning from amino acid 1 through 172 of SEQ ID NO:2 produced in Chinese hamster ovary cells, Trichoplusia ni cells, and Spodoptera frugiperda cells without success. Without being bound by theory, it is believed that PhFcεRIα_(1-176mut) was a better candidate because it apparently represents a complete extracellular domain and it lacked carbohydrates that interfered with complex formation for structural analysis.

[0029] The 3-D model of the complex between PhFcεRIα_(1-176mut) and PhFc-Cε3/Cε4₁₋₂₂₂ is also very surprising in view not only of the knowledge of the structure of proteins containing immunoglobulin domains, herein also referred to as Ig domains, but also in view of the crystal structures of FcεRIα alone, which is disclosed in U.S. patent application Ser. No. 09/434,193, filed Nov. 4, 1999, by Jardetzky et al., and in PCT Publication No. WO 00/26246, published May 11, 2000, by Jardetzky et al., and of Fc-Cε3/Cε4 alone, which is disclosed in U.S. patent application Ser. No. 60/189,403, filed Mar. 15, 2000, by Jardetzky et al. WO 00/26246, ibid., 09/434,193, ibid., and 60/189,403, ibid. are incorporated by reference herein in their entireties. Not only is the structure of FcεRIα in the complex fairly similar to the unique structure of FcεRIα alone, but, even more surprisingly, the structure of Fc-Cε3/Cε4 in the complex is very different from that of Fc-Cε3/Cε4 alone. For example, as disclosed in 60/189,403, ibid., the Fc region of IgE alone exists in a closed conformation whereas receptor-bound IgE Fc exists in an open conformation. The model also predicts that a FcεRIα protein and an IgE Fc region bind at a stoichiometry of 1:1 which is surprising since each Fc region has two Cε3 domains. Comparison of these structural similarities and differences are described in greater detail in the Examples. Analysis of the model which substantially represents the atomic coordinates specified in Table 1 indicates the necessity of such a model for proper interpretation and refinement of mutagenesis and region swapping studies that have been reported. Such a model permits differentiation, even more so than models of FcεRIα alone as disclosed in Ser. No. 09/434,193, ibid., WO 00/26246, ibid., and Garman et al., 1999, Cell 95, 951-961, between amino acids directly or indirectly influencing binding of IgE to FcεRIα and demonstrates where amino acids and amino acid segments identified in mutagenesis and swapping studies are positioned on the protein. By using a model of the present invention one can identify the interactions of FcεRIα and IgE, thereby identifying amino acids to target for mutein production or regions to target for the development of compounds to inhibit binding of IgE to its receptor. Such a model can be used alone or in conjunction with a model of FcεRIα alone (Ser. No. 09/434,193, ibid. or WO 00/26246, ibid.) or Fc-Cε3/Cε4 alone (60/189,403, ibid.).

[0030] One embodiment of the present invention is an isolated crystal of a complex between an extracellular domain of a FcεRIα protein and a Fc-Cε3/Cε4 region of an IgE antibody. As used herein, an isolated crystal is a crystal of a protein that has been produced in a laboratory; that is, an isolated crystal is produced by an individual and is not an object found in situ in nature. It is appreciated by those skilled in the art that there are a variety of techniques to produce crystals including, but not limited to, vapor diffusion using a hanging or sitting drop methodology, vapor diffusion under oil, and batch methods; see, for example, Ducruix et al., eds., 1991, Crystallization of nucleic acids and proteins; A practical approach, Oxford University Press, and Wyckoff et al., eds., 1985, Methods in Enzymology 11, 49-185; each reference is incorporated by reference herein in its entirety. It is also to be appreciated that crystallization conditions can be adjusted depending on a protein's inherent characteristics as well as on a protein's concentration in a solution and that a variety of precipitants can be added to a protein solution in order to effect crystallization; such precipitants are known to those skilled in the art. In a preferred embodiment, a crystal of a complex between an FcεRIα protein and a Fc-Cε3/Cε4 region is produced in a solution by adding a precipitant such as polyethylene glycol (PEG) or PEG monomethylether. In one embodiment, a crystal of the present invention is produced in the presence of 3-[3-(cholamidopropyl) dimethylammonio]-1-propane-sulfonate (CHAPS), or a similar detergent. It is also to be noted that a FcεRIα protein and Fc-Cε3/CCε4 region used to produce a crystal can be produced by a variety of methods, including purification of a native protein, chemical synthesis of a protein, or recombinant production of a protein. Although a number of cell types can be used to recombinantly produce such a protein, insect cells, such as, but not limited to Trichoplusia ni and Spodoptera frugiperda, are preferred, with Trichoplusia ni cells being more preferred. Additional methods to produce proteins are disclosed below.

[0031] Isolated crystals of the present invention can include heavy atom derivatives, such as, but not limited to, gold, platinum, mercury, selenium, copper, and lead. Such heavy atoms can be introduced randomly or introduced in a manner based on knowledge of 3-D models of the present invention. Additional crystals of the present invention are not derivatized. In one embodiment, an isolated crystal of the present invention is a co-crystal of a FcεRIα protein bound to a Fc domain of an IgE antibody in the presence of a compound that inhibits the binding of a FcεRIα protein to a Fc domain of an IgE antibody. Additional crystals of the present invention include crystals produced from proteins that are muteins of the present invention or other proteins that are represented by a 3-D model of the present invention.

[0032] An isolated crystal of the present invention can be the crystal of a complex between any suitable extracellular domain of a FcεRIα protein and a Fc region that binds to FcεRIα, such as a Fe comprising Cε3 domains or a Fe comprising Cε3 and Cε4 domains. Suitable FcεRIα proteins include mammalian FcεRIα proteins, with human, canine, feline, equine, rat and murine FcεRIα proteins being preferred, and human FcεRIα proteins being even more preferred. Suitable Fc-Cε3/Cε4 regions include mammalian Fc-Cε3/Cε4 regions, proteins, with human, canine, feline, equine, rat and murine Fc-Cε3/Cε4 regions being preferred, and human Fc-Cε3/Cε4 regions being even more preferred. A preferred crystal of the present invention diffracts X-rays to a resolution of about 4.5 angstroms or higher (i.e., lower number meaning higher resolution), with resolutions of about 4.0 angstroms or higher, about 3.5 angstroms or higher, about 3.25 angstroms or higher, about 3 angstroms or higher, about 2.5 angstroms or higher, about 2 angstroms or higher, about 1.5 angstroms or higher, and about 1 angstrom or higher being increasingly more preferred. It is appreciated, however, that additional crystals of lower resolutions can have utility in discerning overall topology of the structures, e.g., location of a binding site or where a molecule binds to a receptor or to an antibody. A particularly preferred isolated crystal of the present invention has the amino acid sequence SEQ ID NO:2, amino acid sequence SEQ ID NO:4, or a sequence essentially equivalent that represents an extracellular domain of another mammalian FcεRIα protein in complex with a Fc-Cε3/Cε4 region having amino acid sequence SEQ ID NO:6, or a sequence essentially equivalent that represents another mammalian Fe-Cε3/Cε4 region. Preferred are crystals that belong to spacegroup P4₁2₁2 or spacegroup R32. Particularly preferred crystals include: a crystal belonging to spacegroup P4₁2₁2 that has cell dimensions of 126 angstroms×126 angstroms×129 angstroms and that diffracts X-rays to a resolution of about 4.5 angstroms; and a crystal belonging to spacegroup R32 that has cell dimensions of 192.8 angstroms×192.8 angstroms×302 angstroms and that diffracts X-rays to a resolution of about 3.25 angstroms.

[0033] The present invention includes a 3-D model of a complex between an extracellular domain of a FcεRIα protein and a Fc-Cε3/Cε4 region that substantially represents the atomic coordinates specified in Table 1. The present invention also includes 3-D models that comprise modifications of the model substantially represented by the atomic coordinates specified in Table 1. Each such modification represents a complex between a Fc receptor protein that binds to a Fc domain of an antibody and an antibody Fc region that binds to a Fc receptor protein. A 3-D model of a complex between an extracellular domain of a FcεRIα protein and a Fc-Cε3/Cε4 region is a representation, or image, that predicts the actual structure of the corresponding complex. As such, a 3-D model is a tool that can be used to probe the relationship between the complex's structure and function at the atomic level and to design muteins (i.e., genetically and/or chemically altered FcRs or antibodies) having an improved function, such as, but not limited to: increased (i.e., enhanced) stability; increased antibody or FcR, respectively, binding activity, for example, by, increasing the affinity for an antibody or FcR, respectively, by, for example, increasing the association rate and/or decreasing the dissociation rate between a FcR and an antibody or by altering substrate specificity (e.g., enhancing the ability of a FcR of a certain species and class to bind to antibody from another species and/or another antibody class); and/or increased solubility (e.g., reduced aggregation). It is well known to those skilled in the art, however, that a 3-D model of a protein or a complex derived by analysis of protein or complex crystals is not identical to the inherent structure of the protein or complex. See, for example, Branden et al., Introduction to Protein Structure, Garland Publishing Inc., New York and London, 1991, especially on page 277, which states “not surprisingly the model never corresponds precisely to the actual crystal.” Furthermore, the model can be subjected to further refinements to more closely correspond to the actual structure of a complex between a FcR and antibody. Such a refined model, which is an example of a modification of the present invention, is a better predictor of the actual structure and mechanism of action of the complex that the model represents. A refinement of a 3-D model of the present invention refers to an improved model of a complex between an extracellular domain of a FcεRIα protein and a Fc-Cε3/Cε4 region that can be obtained in a variety of ways known to those skilled in the art. Refinements can include models determined to more preferred degrees of resolution, preferably to about 4.5 angstroms, more preferably to about 4 angstroms, more preferably to about 3.5 angstroms, more preferably to about 3.25 angstroms, more preferably to about 3 angstroms, more preferably to about 2.5 angstroms, more preferably to about 2 angstroms, more preferably to about 1.5 angstroms, and even more preferably to about 1 angstrom. Preferred refinements are obtained using the 3-D model as a basis for such improvements.

[0034] One embodiment of the present invention is a 3-D model of a complex between an extracellular domain of a FcεRIα protein and a Fc-Cε3/Cε4 region that substantially represents the atomic coordinates specified (i.e., listed) in Table 1. TABLE 1 Atomic coordinates of com14i_deposit.pdb ATOM ATOM # TYPE RES CHN # X Y Z OCC B 1 CB VAL A 1 −3.308 77.955 157.480 1.00 54.19 2 CG1 VAL A 1 −2.631 78.371 156.184 1.00 159.57 3 CG2 VAL A 1 −3.131 76.460 157.704 1.00 132.31 4 C VAL A 1 −2.948 80.258 158.492 1.00 178.97 5 O VAL A 1 −2.487 80.838 157.504 1.00 201.24 6 N VAL A 1 −3.255 78.193 159.967 1.00 154.76 7 CA VAL A 1 −2.715 78.740 158.688 1.00 168.39 8 N PRO A 2 −3.652 80.926 159.432 1.00 162.09 9 CD PRO A 2 −4.400 80.420 160.599 1.00 80.92 10 CA PRO A 2 −3.883 82.370 159.264 1.00 154.66 11 CB PRO A 2 −5.040 82.635 160.223 1.00 150.00 12 CG PRO A 2 −4.741 81.687 161.341 1.00 74.00 13 C PRO A 2 −2.659 83.238 159.588 1.00 157.76 14 O PRO A 2 −1.561 82.723 159.805 1.00 153.79 15 N GLN A 3 −2.850 84.557 159.604 1.00 167.42 16 CA GLN A 3 −1.767 85.480 159.940 1.00 118.16 17 CB GLN A 3 −2.084 86.902 159.460 1.00 89.25 18 CG GLN A 3 −1.705 87.173 158.009 1.00 165.02 19 CD GLN A 3 −2.117 88.561 157.535 1.00 182.69 20 OE1 GLN A 3 −1.725 89.570 158.120 1.00 146.97 21 NE2 GLN A 3 −2.908 88.616 156.462 1.00 178.25 22 C GLN A 3 −1.604 85.479 161.457 1.00 111.63 23 O GLN A 3 −2.582 85.634 162.192 1.00 63.56 24 N LYS A 4 −0.370 85.284 161.916 1.00 119.89 25 CA LYS A 4 −0.062 85.264 163.344 1.00 60.75 26 CB LYS A 4 1.263 84.535 163.607 1.00 99.96 27 CG LYS A 4 1.320 83.103 163.084 1.00 192.75 28 CD LYS A 4 2.645 82.417 163.434 1.00 187.23 29 CE LYS A 4 2.670 80.974 162.925 1.00 187.05 30 NZ LYS A 4 3.932 80.256 163.268 1.00 160.49 31 C LYS A 4 0.069 86.705 163.805 1.00 68.75 32 O LYS A 4 0.179 87.615 162.990 1.00 95.41 33 N PRO A 5 0.051 86.938 165.121 1.00 28.76 34 CD PRO A 5 −0.398 86.034 166.189 1.00 61.76 35 CA PRO A 5 0.176 88.304 165.632 1.00 48.28 36 CB PRO A 5 −0.576 88.231 166.949 1.00 43.06 37 CG PRO A 5 −0.226 86.882 167.417 1.00 11.05 38 C PRO A 5 1.638 88.734 165.804 1.00 63.30 39 O PRO A 5 2.469 87.967 166.293 1.00 54.45 40 N LYS A 6 1.944 89.961 165.388 1.00 63.56 41 CA LYS A 6 3.304 90.497 165.470 1.00 95.51 42 CB LYS A 6 3.647 91.212 164.151 1.00 110.28 43 CG LYS A 6 5.083 91.745 164.040 1.00 190.76 44 CD LYS A 6 6.120 90.634 163.856 1.00 206.32 45 CE LYS A 6 7.533 91.195 163.662 1.00 184.83 46 NZ LYS A 6 7.695 91.956 162.385 1.00 173.73 47 C LYS A 6 3.467 91.461 166.658 1.00 86.34 48 O LYS A 6 2.486 92.000 167.156 1.00 52.28 49 N VAL A 7 4.706 91.655 167.118 1.00 90.20 50 CA VAL A 7 5.010 92.561 168.234 1.00 22.49 51 CB VAL A 7 5.718 91.859 169.380 1.00 13.79 52 CG1 VAL A 7 4.920 92.017 170.651 1.00 31.43 53 CG2 VAL A 7 5.937 90.401 169.033 1.00 92.97 54 C VAL A 7 5.970 93.614 167.743 1.00 46.84 55 O VAL A 7 6.960 93.293 167.084 1.00 64.82 56 N SER A 8 5.680 94.867 168.065 1.00 36.46 57 CA SER A 8 6.527 95.968 167.652 1.00 64.14 58 CB SER A 8 5.721 96.962 166.816 1.00 31.16 59 OG SER A 8 4.731 97.609 167.600 1.00 112.57 60 C SER A 8 7.100 96.651 168.898 1.00 70.84 61 O SER A 8 6.467 96.688 169.957 1.00 65.38 62 N LEU A 9 8.311 97.173 168.772 1.00 34.20 63 CA LEU A 9 8.962 97.844 169.877 1.00 17.68 64 CB LEU A 9 10.335 97.254 170.082 1.00 35.73 65 CG LEU A 9 10.470 95.929 170.799 1.00 5.42 66 CD1 LEU A 9 11.720 95.218 170.359 1.00 46.16 67 CD2 LEU A 9 10.552 96.200 172.244 1.00 38.43 68 C LEU A 9 9.127 99.312 169.564 1.00 46.19 69 O LEU A 9 9.420 99.680 168.438 1.00 59.24 70 N ASN A 10 8.948 100.161 170.558 1.00 40.05 71 CA ASN A 10 9.130 101.576 170.325 1.00 38.01 72 CB ASN A 10 7.815 102.221 169.923 1.00 60.50 73 CG ASN A 10 7.972 103.675 169.566 1.00 65.72 74 OD1 ASN A 10 7.555 104.551 170.319 1.00 78.78 75 ND2 ASN A 10 8.588 103.946 168.419 1.00 85.11 76 C ASN A 10 9.683 102.237 171.567 1.00 46.63 77 O ASN A 10 8.989 102.372 172.570 1.00 38.10 78 N PRO A 11 10.952 102.661 171.513 1.00 36.23 79 CD PRO A 11 11.474 103.662 172.446 1.00 18.87 80 CA PRO A 11 11.852 102.543 170.367 1.00 23.13 81 CB PRO A 11 12.980 103.476 170.747 1.00 49.98 82 CG PRO A 11 12.266 104.514 171.534 1.00 45.32 83 C PRO A 11 12.331 101.123 170.053 1.00 52.44 84 O PRO A 11 12.575 100.322 170.964 1.00 41.38 85 N PRO A 12 12.530 100.832 168.752 1.00 25.66 86 CD PRO A 12 12.912 101.992 167.931 1.00 5.42 87 CA PRO A 12 12.961 99.600 168.075 1.00 20.64 88 CB PRO A 12 13.691 100.118 166.845 1.00 15.38 89 CG PRO A 12 13.032 101.395 166.573 1.00 36.22 90 C PRO A 12 13.858 98.688 168.875 1.00 26.86 91 O PRO A 12 13.653 97.480 168.946 1.00 75.83 92 N TRP A 13 14.881 99.297 169.445 1.00 51.05 93 CA TRP A 13 15.898 98.623 170.226 1.00 46.59 94 CB TRP A 13 16.675 99.690 170.966 1.00 5.42 95 CG TRP A 13 16.638 100.993 170.234 1.00 17.98 96 CD2 TRP A 13 16.993 101.221 168.870 1.00 11.54 97 CE2 TRP A 13 16.869 102.602 168.631 1.00 36.13 98 CE3 TRP A 13 17.413 100.392 167.826 1.00 16.34 99 CD1 TRP A 13 16.310 102.211 170.749 1.00 79.53 100 NE1 TRP A 13 16.446 103.183 169.797 1.00 12.94 101 CZ2 TRP A 13 17.158 103.178 167.391 1.00 5.42 102 CZ3 TRP A 13 17.698 100.965 166.596 1.00 58.81 103 CH2 TRP A 13 17.572 102.346 166.393 1.00 14.55 104 C TRP A 13 15.357 97.588 171.200 1.00 53.67 105 O TRP A 13 14.615 97.929 172.116 1.00 40.75 106 N ASN A 14 15.726 96.326 171.003 1.00 40.23 107 CA ASN A 14 15.272 95.289 171.905 1.00 39.68 108 CB ASN A 14 14.910 94.012 171.148 1.00 55.19 109 CG ASN A 14 15.994 93.556 170.225 1.00 52.50 110 OD1 ASN A 14 17.116 93.309 170.653 1.00 34.32 111 ND2 ASN A 14 15.668 93.437 168.940 1.00 84.53 112 C ASN A 14 16.328 95.017 172.956 1.00 39.79 113 O ASN A 14 16.232 94.049 173.704 1.00 68.24 114 N ARG A 15 17.344 95.876 172.992 1.00 42.06 115 CA ARG A 15 18.420 95.815 173.989 1.00 51.52 116 CB ARG A 15 19.738 95.306 173.392 1.00 16.41 117 CG ARG A 15 20.077 95.790 172.006 1.00 43.90 118 CD ARG A 15 21.494 95.348 171.646 1.00 69.87 119 NE ARG A 15 21.733 93.931 171.916 1.00 49.77 120 CZ ARG A 15 22.922 93.426 172.230 1.00 53.72 121 NH1 ARG A 15 23.985 94.212 172.321 1.00 38.62 122 NH2 ARG A 15 23.050 92.129 172.455 1.00 109.67 123 C ARG A 15 18.581 97.235 174.499 1.00 19.10 124 O ARG A 15 18.822 98.147 173.725 1.00 10.96 125 N ILE A 16 18.440 97.420 175.802 1.00 22.57 126 CA ILE A 16 18.502 98.752 176.385 1.00 22.94 127 CB ILE A 16 17.101 99.298 176.601 1.00 32.81 128 CG2 ILE A 16 16.463 99.668 175.286 1.00 35.27 129 CG1 ILE A 16 16.283 98.250 177.349 1.00 10.08 130 CD1 ILE A 16 14.931 98.711 177.716 1.00 45.93 131 C ILE A 16 19.170 98.826 177.745 1.00 47.61 132 O ILE A 16 19.175 97.854 178.495 1.00 52.58 133 N PHE A 17 19.693 100.003 178.070 1.00 19.08 134 CA PHE A 17 20.332 100.224 179.361 1.00 30.02 135 CB PHE A 17 20.977 101.603 179.405 1.00 34.47 136 CG PHE A 17 22.216 101.709 178.604 1.00 34.70 137 CD1 PHE A 17 22.493 102.868 177.889 1.00 48.32 138 CD2 PHE A 17 23.105 100.649 178.544 1.00 11.47 139 CE1 PHE A 17 23.633 102.972 177.121 1.00 16.41 140 CE2 PHE A 17 24.246 100.739 177.782 1.00 40.21 141 CZ PHE A 17 24.513 101.904 177.065 1.00 105.94 142 C PHE A 17 19.282 100.153 180.456 1.00 37.78 143 O PHE A 17 18.146 100.564 180.256 1.00 17.05 144 N LYS A 18 19.661 99.662 181.624 1.00 5.42 145 CA LYS A 18 18.702 99.583 182.696 1.00 38.72 146 CB LYS A 18 19.318 98.921 183.931 1.00 15.58 147 CG LYS A 18 19.768 99.862 185.000 1.00 22.71 148 CD LYS A 18 20.290 99.109 186.226 1.00 39.40 149 CE LYS A 18 19.181 98.710 187.181 1.00 57.95 150 NZ LYS A 18 19.692 98.586 188.585 1.00 58.03 151 C LYS A 18 18.213 100.972 183.034 1.00 9.14 152 O LYS A 18 18.976 101.919 183.006 1.00 14.56 153 N GLY A 19 16.928 101.071 183.353 1.00 48.65 154 CA GLY A 19 16.338 102.342 183.702 1.00 37.66 155 C GLY A 19 15.760 103.020 182.487 1.00 11.50 156 O GLY A 19 15.196 104.106 182.580 1.00 82.09 157 N GLU A 20 15.916 102.389 181.332 1.00 51.25 158 CA GLU A 20 15.390 102.959 180.101 1.00 39.98 159 CB GLU A 20 16.245 102.547 178.901 1.00 61.38 160 CG GLU A 20 17.645 103.141 178.937 1.00 107.42 161 CD GLU A 20 18.374 103.073 177.608 1.00 75.17 162 OE1 GLU A 20 19.490 103.620 177.537 1.00 70.97 163 OE2 GLU A 20 17.847 102.483 176.639 1.00 72.76 164 C GLU A 20 13.950 102.532 179.893 1.00 47.68 165 O GLU A 20 13.449 101.624 180.565 1.00 16.47 166 N ASN A 21 13.280 103.200 178.964 1.00 51.83 167 CA ASN A 21 11.885 102.910 178.692 1.00 39.65 168 CB ASN A 21 11.057 104.195 178.786 1.00 36.44 169 CG ASN A 21 11.008 104.762 180.191 1.00 24.19 170 OD1 ASN A 21 10.954 104.009 181.164 1.00 25.70 171 ND2 ASN A 21 11.002 106.089 180.298 1.00 72.05 172 C ASN A 21 11.653 102.271 177.340 1.00 14.38 173 O ASN A 21 12.362 102.554 176.384 1.00 96.93 174 N VAL A 22 10.651 101.405 177.270 1.00 55.87 175 CA VAL A 22 10.305 100.748 176.023 1.00 39.97 176 CB VAL A 22 11.168 99.525 175.769 1.00 23.77 177 CG1 VAL A 22 10.880 98.461 176.789 1.00 24.69 178 CG2 VAL A 22 10.896 99.013 174.395 1.00 10.67 179 C VAL A 22 8.861 100.308 176.057 1.00 39.52 180 O VAL A 22 8.299 100.143 177.134 1.00 50.04 181 N THR A 23 8.273 100.106 174.879 1.00 35.08 182 CA THR A 23 6.876 99.689 174.758 1.00 50.38 183 CB THR A 23 5.982 100.883 174.356 1.00 15.46 184 OG1 THR A 23 5.325 101.397 175.515 1.00 51.09 185 CG2 THR A 23 4.944 100.470 173.342 1.00 53.00 186 C THR A 23 6.638 98.564 173.758 1.00 24.12 187 O THR A 23 7.121 98.601 172.629 1.00 33.75 188 N LEU A 24 5.869 97.567 174.170 1.00 32.66 189 CA LEU A 24 5.565 96.463 173.278 1.00 45.63 190 CB LEU A 24 5.754 95.119 173.987 1.00 23.83 191 CG LEU A 24 7.072 94.939 174.739 1.00 28.78 192 CD1 LEU A 24 7.381 93.488 174.933 1.00 19.89 193 CD2 LEU A 24 8.159 95.572 173.969 1.00 5.42 194 C LEU A 24 4.128 96.607 172.822 1.00 44.86 195 O LEU A 24 3.248 96.866 173.635 1.00 52.63 196 N THR A 25 3.895 96.444 171.523 1.00 52.39 197 CA THR A 25 2.554 96.550 170.965 1.00 46.08 198 CB THR A 25 2.454 97.761 170.049 1.00 24.50 199 OG1 THR A 25 3.088 98.884 170.673 1.00 62.13 200 CG2 THR A 25 1.016 98.098 169.807 1.00 77.17 201 C THR A 25 2.233 95.282 170.174 1.00 59.55 202 O THR A 25 3.120 94.707 169.542 1.00 36.44 203 N CYS A 26 0.970 94.852 170.215 1.00 59.40 204 CA CYS A 26 0.520 93.642 169.525 1.00 38.53 205 C CYS A 26 −0.343 94.009 168.318 1.00 42.63 206 O CYS A 26 −1.322 94.734 168.447 1.00 77.67 207 CB CYS A 26 −0.256 92.757 170.514 1.00 31.91 208 SG CYS A 26 −0.296 90.939 170.208 1.00 112.14 209 N ASN A 27 0.083 93.514 167.154 1.00 114.86 210 CA ASN A 27 −0.506 93.677 165.805 1.00 124.26 211 CB ASN A 27 −0.765 92.286 165.217 1.00 138.85 212 CG ASN A 27 −0.588 92.249 163.708 1.00 187.97 213 OD1 ASN A 27 −0.071 93.196 163.106 1.00 180.59 214 ND2 ASN A 27 −0.999 91.145 163.090 1.00 211.12 215 C ASN A 27 −1.717 94.563 165.469 1.00 69.87 216 O ASN A 27 −2.604 94.788 166.278 1.00 99.87 217 N GLY A 28 −1.737 95.043 164.228 1.00 93.93 218 CA GLY A 28 −2.818 95.887 163.752 1.00 33.38 219 C GLY A 28 −3.811 95.070 162.949 1.00 71.27 220 O GLY A 28 −4.658 95.611 162.243 1.00 61.63 221 N ASN A 29 −3.686 93.752 163.064 1.00 116.52 222 CA ASN A 29 −4.550 92.783 162.388 1.00 70.71 223 CB ASN A 29 −3.729 91.533 162.062 1.00 121.95 224 CG ASN A 29 −4.164 90.852 160.783 1.00 150.49 225 OD1 ASN A 29 −4.247 91.480 159.727 1.00 172.84 226 ND2 ASN A 29 −4.428 89.550 160.868 1.00 174.68 227 C ASN A 29 −5.658 92.466 163.405 1.00 97.53 228 O ASN A 29 −6.252 91.389 163.421 1.00 106.16 229 N ASN A 30 −5.886 93.448 164.265 1.00 53.59 230 CA ASN A 30 −6.878 93.432 165.332 1.00 80.30 231 CB ASN A 30 −6.317 92.689 166.558 1.00 85.88 232 CG ASN A 30 −7.040 93.041 167.875 1.00 109.70 233 OD1 ASN A 30 −8.256 92.883 168.011 1.00 70.68 234 ND2 ASN A 30 −6.272 93.507 168.851 1.00 35.68 235 C ASN A 30 −7.041 94.917 165.623 1.00 78.22 236 O ASN A 30 −6.772 95.363 166.729 1.00 51.75 237 N PHE A 31 −7.493 95.667 164.617 1.00 89.72 238 CA PHE A 31 −7.629 97.125 164.709 1.00 96.61 239 CB PHE A 31 −7.900 97.716 163.320 1.00 115.42 240 CG PHE A 31 −7.680 99.211 163.242 1.00 120.39 241 CD1 PHE A 31 −6.403 99.745 163.398 1.00 112.19 242 CD2 PHE A 31 −8.746 100.083 163.023 1.00 119.97 243 CE1 PHE A 31 −6.190 101.121 163.339 1.00 72.84 244 CE2 PHE A 31 −8.544 101.460 162.962 1.00 60.99 245 CZ PHE A 31 −7.262 101.978 163.122 1.00 105.12 246 C PHE A 31 −8.585 97.783 165.707 1.00 94.85 247 O PHE A 31 −8.131 98.494 166.601 1.00 127.53 248 N PHE A 32 −9.894 97.596 165.564 1.00 91.11 249 CA PHE A 32 −10.818 98.248 166.500 1.00 92.26 250 CB PHE A 32 −12.272 98.103 166.052 1.00 93.61 251 CG PHE A 32 −12.504 98.467 164.625 1.00 103.12 252 CD1 PHE A 32 −12.136 97.591 163.600 1.00 99.09 253 CD2 PHE A 32 −13.064 99.693 164.298 1.00 32.51 254 CE1 PHE A 32 −12.320 97.933 162.268 1.00 63.07 255 CE2 PHE A 32 −13.251 100.044 162.974 1.00 108.41 256 CZ PHE A 32 −12.877 99.160 161.953 1.00 118.33 257 C PHE A 32 −10.673 97.618 167.867 1.00 102.23 258 O PHE A 32 −11.305 98.050 168.838 1.00 76.95 259 N GLU A 33 −9.827 96.593 167.918 1.00 90.59 260 CA GLU A 33 −9.567 95.837 169.127 1.00 58.80 261 CB GLU A 33 −9.193 96.766 170.287 1.00 34.16 262 CG GLU A 33 −7.709 97.116 170.319 1.00 83.37 263 CD GLU A 33 −7.302 97.846 171.583 1.00 138.46 264 OE1 GLU A 33 −7.822 97.498 172.666 1.00 156.92 265 OE2 GLU A 33 −6.450 98.757 171.494 1.00 143.48 266 C GLU A 33 −10.807 95.038 169.458 1.00 51.35 267 O GLU A 33 −11.670 95.489 170.207 1.00 76.71 268 N VAL A 34 −10.889 93.849 168.874 1.00 40.24 269 CA VAL A 34 −12.018 92.963 169.092 1.00 63.51 270 CB VAL A 34 −12.369 92.212 167.815 1.00 12.87 271 CG1 VAL A 34 −12.724 93.199 166.743 1.00 47.66 272 CG2 VAL A 34 −11.194 91.350 167.382 1.00 80.18 273 C VAL A 34 −11.691 91.960 170.185 1.00 48.93 274 O VAL A 34 −12.584 91.300 170.719 1.00 66.41 275 N SER A 35 −10.411 91.840 170.518 1.00 40.51 276 CA SER A 35 −10.027 90.913 171.568 1.00 79.37 277 CB SER A 35 −9.460 89.642 170.974 1.00 33.93 278 OG SER A 35 −8.107 89.851 170.650 1.00 44.80 279 C SER A 35 −8.991 91.484 172.530 1.00 83.70 280 O SER A 35 −8.097 92.242 172.139 1.00 52.41 281 N SER A 36 −9.127 91.112 173.798 1.00 57.27 282 CA SER A 36 −8.195 91.539 174.819 1.00 23.32 283 CB SER A 36 −8.600 90.956 176.156 1.00 119.43 284 OG SER A 36 −8.593 89.547 176.089 1.00 43.01 285 C SER A 36 −6.879 90.929 174.408 1.00 49.51 286 O SER A 36 −6.857 89.930 173.702 1.00 34.96 287 N THR A 37 −5.780 91.517 174.854 1.00 52.38 288 CA THR A 37 −4.466 90.996 174.516 1.00 34.52 289 CB THR A 37 −3.501 92.113 174.181 1.00 28.99 290 OG1 THR A 37 −4.074 92.965 173.182 1.00 95.55 291 CG2 THR A 37 −2.211 91.537 173.682 1.00 68.24 292 C THR A 37 −3.890 90.283 175.710 1.00 57.63 293 O THR A 37 −4.159 90.662 176.848 1.00 34.77 294 N LYS A 38 −3.109 89.241 175.469 1.00 28.90 295 CA LYS A 38 −2.491 88.551 176.588 1.00 65.81 296 CB LYS A 38 −3.111 87.179 176.799 1.00 34.97 297 CG LYS A 38 −3.818 86.631 175.615 1.00 36.39 298 CD LYS A 38 −5.098 85.965 176.076 1.00 85.18 299 CE LYS A 38 −6.234 86.958 176.203 1.00 26.12 300 NZ LYS A 38 −7.146 86.806 175.029 1.00 20.00 301 C LYS A 38 −0.990 88.454 176.381 1.00 79.44 302 O LYS A 38 −0.523 87.805 175.444 1.00 44.12 303 N TRP A 39 −0.256 89.130 177.268 1.00 74.45 304 CA TRP A 39 1.198 89.204 177.230 1.00 12.82 305 CB TRP A 39 1.656 90.574 177.704 1.00 55.75 306 CG TRP A 39 1.180 91.696 176.875 1.00 17.73 307 CD2 TRP A 39 1.763 92.144 175.661 1.00 20.84 308 CE2 TRP A 39 0.957 93.195 175.175 1.00 24.82 309 CE3 TRP A 39 2.889 91.757 174.930 1.00 15.24 310 CD1 TRP A 39 0.069 92.473 177.082 1.00 45.58 311 NE1 TRP A 39 −0.072 93.374 176.060 1.00 18.25 312 CZ2 TRP A 39 1.247 93.864 173.990 1.00 26.70 313 CZ3 TRP A 39 3.177 92.419 173.751 1.00 13.49 314 CH2 TRP A 39 2.360 93.463 173.293 1.00 70.81 315 C TRP A 39 1.847 88.166 178.109 1.00 55.49 316 O TRP A 39 1.417 87.945 179.236 1.00 33.26 317 N PHE A 40 2.916 87.566 177.604 1.00 28.08 318 CA PHE A 40 3.640 86.538 178.331 1.00 19.83 319 CB PHE A 40 3.527 85.229 177.574 1.00 69.82 320 CG PHE A 40 2.137 84.682 177.528 1.00 65.09 321 CD1 PHE A 40 1.608 84.205 176.338 1.00 50.58 322 CD2 PHE A 40 1.367 84.614 178.680 1.00 53.63 323 CE1 PHE A 40 0.341 83.673 176.300 1.00 68.98 324 CE2 PHE A 40 0.105 84.083 178.646 1.00 26.70 325 CZ PHE A 40 −0.414 83.611 177.459 1.00 85.38 326 C PHE A 40 5.112 86.889 178.522 1.00 83.34 327 O PHE A 40 5.835 87.108 177.546 1.00 65.61 328 N HIS A 41 5.549 86.924 179.780 1.00 49.52 329 CA HIS A 41 6.929 87.243 180.121 1.00 41.84 330 CB HIS A 41 6.950 88.359 181.166 1.00 82.94 331 CG HIS A 41 8.325 88.832 181.529 1.00 109.26 332 CD2 HIS A 41 8.822 89.302 182.698 1.00 54.39 333 ND1 HIS A 41 9.361 88.901 180.618 1.00 50.58 334 CE1 HIS A 41 10.433 89.389 181.213 1.00 51.90 335 NE2 HIS A 41 10.133 89.642 182.475 1.00 80.09 336 C HIS A 41 7.671 86.006 180.630 1.00 66.77 337 O HIS A 41 7.413 85.511 181.729 1.00 49.22 338 N ASN A 42 8.594 85.513 179.806 1.00 91.49 339 CA ASN A 42 9.383 84.329 180.122 1.00 83.79 340 CB ASN A 42 10.313 84.601 181.315 1.00 71.40 341 CG ASN A 42 11.573 85.360 180.915 1.00 72.11 342 OD1 ASN A 42 11.498 86.390 180.243 1.00 85.40 343 ND2 ASN A 42 12.732 84.857 181.333 1.00 104.80 344 C ASN A 42 8.464 83.156 180.421 1.00 77.24 345 O ASN A 42 8.923 82.037 180.657 1.00 110.53 346 N GLY A 43 7.162 83.418 180.389 1.00 47.35 347 CA GLY A 43 6.201 82.378 180.662 1.00 34.83 348 C GLY A 43 4.909 82.844 181.300 1.00 49.78 349 O GLY A 43 3.855 82.683 180.707 1.00 48.66 350 N SER A 44 4.971 83.412 182.499 1.00 38.80 351 CA SER A 44 3.760 83.860 183.181 1.00 51.26 352 CB SER A 44 4.090 84.455 184.553 1.00 115.68 353 OG SER A 44 4.024 83.466 185.572 1.00 158.60 354 C SER A 44 2.933 84.859 182.407 1.00 57.42 355 O SER A 44 3.443 85.594 181.569 1.00 48.28 356 N LEU A 45 1.639 84.871 182.708 1.00 78.92 357 CA LEU A 45 0.698 85.769 182.062 1.00 43.70 358 CB LEU A 45 −0.728 85.215 182.177 1.00 33.26 359 CG LEU A 45 −1.810 86.048 181.475 1.00 38.67 360 CD1 LEU A 45 −1.934 85.532 180.084 1.00 20.12 361 CD2 LEU A 45 −3.171 85.962 182.155 1.00 16.35 362 C LEU A 45 0.755 87.134 182.731 1.00 45.32 363 O LEU A 45 0.531 87.243 183.928 1.00 46.93 364 N SER A 46 1.053 88.176 181.964 1.00 43.39 365 CA SER A 46 1.100 89.513 182.530 1.00 61.73 366 CB SER A 46 1.808 90.469 181.584 1.00 36.13 367 OG SER A 46 1.827 91.769 182.137 1.00 89.66 368 C SER A 46 −0.316 90.006 182.778 1.00 33.11 369 O SER A 46 −1.245 89.564 182.105 1.00 74.17 370 N GLU A 47 −0.475 90.927 183.727 1.00 51.16 371 CA GLU A 47 −1.794 91.467 184.059 1.00 59.94 372 CB GLU A 47 −1.876 91.906 185.536 1.00 102.95 373 CG GLU A 47 −1.109 93.176 185.915 1.00 167.20 374 CD GLU A 47 −1.380 93.622 187.356 1.00 181.03 375 OE1 GLU A 47 −2.558 93.869 187.696 1.00 179.85 376 OE2 GLU A 47 −0.420 93.729 188.151 1.00 185.11 377 C GLU A 47 −2.257 92.613 183.169 1.00 72.12 378 O GLU A 47 −3.330 93.173 183.399 1.00 64.78 379 N GLU A 48 −1.459 92.977 182.168 1.00 30.89 380 CA GLU A 48 −1.875 94.033 181.255 1.00 56.44 381 CB GLU A 48 −0.689 94.737 180.606 1.00 83.36 382 CG GLU A 48 −1.099 95.797 179.581 1.00 51.54 383 CD GLU A 48 −1.832 96.978 180.201 1.00 104.67 384 OE1 GLU A 48 −2.168 96.919 181.403 1.00 138.97 385 OE2 GLU A 48 −2.077 97.968 179.481 1.00 142.55 386 C GLU A 48 −2.664 93.332 180.178 1.00 67.47 387 O GLU A 48 −2.224 92.303 179.658 1.00 72.45 388 N THR A 49 −3.827 93.874 179.841 1.00 44.94 389 CA THR A 49 −4.650 93.249 178.824 1.00 53.65 390 CB THR A 49 −6.057 92.937 179.361 1.00 38.32 391 OG1 THR A 49 −6.717 94.152 179.731 1.00 71.69 392 CG2 THR A 49 −5.957 92.031 180.574 1.00 68.17 393 C THR A 49 −4.773 94.090 177.570 1.00 42.57 394 O THR A 49 −5.323 93.620 176.572 1.00 55.30 395 N ASN A 50 −4.244 95.316 177.618 1.00 39.30 396 CA ASN A 50 −4.308 96.238 176.481 1.00 35.89 397 CB ASN A 50 −4.131 97.680 176.959 1.00 40.10 398 CG ASN A 50 −5.248 98.123 177.888 1.00 104.98 399 OD1 ASN A 50 −6.425 97.966 177.566 1.00 104.75 400 ND2 ASN A 50 −4.888 98.684 179.044 1.00 117.05 401 C ASN A 50 −3.331 95.925 175.343 1.00 40.37 402 O ASN A 50 −2.419 95.117 175.484 1.00 38.49 403 N SER A 51 −3.545 96.576 174.208 1.00 50.20 404 CA SER A 51 −2.751 96.358 173.012 1.00 23.03 405 CB SER A 51 −3.377 97.148 171.867 1.00 91.07 406 OG SER A 51 −2.997 96.611 170.612 1.00 171.49 407 C SER A 51 −1.259 96.682 173.121 1.00 69.60 408 O SER A 51 −0.437 96.164 172.360 1.00 46.29 409 N SER A 52 −0.896 97.547 174.055 1.00 45.59 410 CA SER A 52 0.504 97.893 174.211 1.00 54.59 411 CB SER A 52 0.768 99.315 173.715 1.00 8.18 412 OG SER A 52 −0.152 100.219 174.304 1.00 136.82 413 C SER A 52 0.905 97.753 175.661 1.00 27.90 414 O SER A 52 0.190 98.183 176.556 1.00 44.58 415 N LEU A 53 2.053 97.118 175.870 1.00 63.94 416 CA LEU A 53 2.613 96.882 177.188 1.00 46.87 417 CB LEU A 53 3.060 95.430 177.306 1.00 46.27 418 CG LEU A 53 3.830 95.066 178.569 1.00 30.42 419 CD1 LEU A 53 2.999 95.372 179.782 1.00 91.21 420 CD2 LEU A 53 4.172 93.618 178.534 1.00 12.37 421 C LEU A 53 3.811 97.789 177.394 1.00 56.10 422 O LEU A 53 4.693 97.864 176.539 1.00 60.76 423 N ASN A 54 3.841 98.474 178.529 1.00 47.36 424 CA ASN A 54 4.937 99.378 178.841 1.00 46.29 425 CB ASN A 54 4.403 100.640 179.506 1.00 42.78 426 CG ASN A 54 3.436 101.383 178.631 1.00 41.09 427 OD1 ASN A 54 3.786 101.807 177.538 1.00 49.17 428 ND2 ASN A 54 2.207 101.545 179.104 1.00 84.48 429 C ASN A 54 5.976 98.749 179.753 1.00 33.11 430 O ASN A 54 5.771 97.691 180.331 1.00 62.93 431 N ILE A 55 7.106 99.422 179.867 1.00 61.10 432 CA ILE A 55 8.189 98.981 180.719 1.00 47.90 433 CB ILE A 55 9.217 98.157 179.946 1.00 13.22 434 CG2 ILE A 55 10.449 97.922 180.795 1.00 78.62 435 CG1 ILE A 55 8.619 96.807 179.586 1.00 27.07 436 CD1 ILE A 55 9.649 95.826 179.074 1.00 30.03 437 C ILE A 55 8.829 100.267 181.189 1.00 83.99 438 O ILE A 55 9.222 101.101 180.371 1.00 75.43 439 N VAL A 56 8.923 100.443 182.501 1.00 33.41 440 CA VAL A 56 9.505 101.660 183.024 1.00 49.06 441 CB VAL A 56 8.444 102.453 183.758 1.00 15.18 442 CG1 VAL A 56 9.046 103.714 184.329 1.00 108.22 443 CG2 VAL A 56 7.328 102.792 182.789 1.00 29.46 444 C VAL A 56 10.706 101.421 183.923 1.00 69.57 445 O VAL A 56 10.757 100.422 184.648 1.00 49.84 446 N ASN A 57 11.664 102.348 183.872 1.00 28.08 447 CA ASN A 57 12.887 102.233 184.656 1.00 76.91 448 CB ASN A 57 12.673 102.732 186.090 1.00 41.01 449 CG ASN A 57 12.080 104.137 186.133 1.00 126.97 450 OD1 ASN A 57 12.275 104.939 185.212 1.00 85.74 451 ND2 ASN A 57 11.359 104.444 187.211 1.00 113.52 452 C ASN A 57 13.219 100.756 184.636 1.00 51.64 453 O ASN A 57 13.382 100.110 185.669 1.00 51.28 454 N ALA A 58 13.294 100.237 183.419 1.00 5.42 455 CA ALA A 58 13.562 98.838 183.185 1.00 28.33 456 CB ALA A 58 13.971 98.636 181.763 1.00 26.01 457 C ALA A 58 14.604 98.236 184.083 1.00 26.51 458 O ALA A 58 15.769 98.571 183.983 1.00 45.62 459 N LYS A 59 14.182 97.336 184.962 1.00 54.38 460 CA LYS A 59 15.114 96.654 185.838 1.00 54.01 461 CB LYS A 59 14.388 96.159 187.080 1.00 49.09 462 CG LYS A 59 15.301 95.437 188.061 1.00 140.01 463 CD LYS A 59 16.432 96.316 188.603 1.00 80.75 464 CE LYS A 59 17.313 95.516 189.541 1.00 71.72 465 NZ LYS A 59 17.864 94.316 188.836 1.00 63.79 466 C LYS A 59 15.681 95.481 185.031 1.00 38.80 467 O LYS A 59 15.234 95.229 183.920 1.00 40.61 468 N PHE A 60 16.673 94.771 185.549 1.00 36.75 469 CA PHE A 60 17.207 93.658 184.776 1.00 26.24 470 CB PHE A 60 18.416 93.052 185.445 1.00 43.58 471 CG PHE A 60 19.579 93.957 185.491 1.00 76.01 472 CD1 PHE A 60 19.616 95.002 186.399 1.00 61.74 473 CD2 PHE A 60 20.634 93.787 184.606 1.00 45.10 474 CE1 PHE A 60 20.691 95.867 186.419 1.00 50.78 475 CE2 PHE A 60 21.712 94.651 184.621 1.00 21.53 476 CZ PHE A 60 21.741 95.689 185.525 1.00 37.49 477 C PHE A 60 16.169 92.580 184.653 1.00 69.55 478 O PHE A 60 16.062 91.924 183.617 1.00 29.04 479 N GLU A 61 15.429 92.395 185.742 1.00 35.52 480 CA GLU A 61 14.371 91.406 185.823 1.00 48.73 481 CB GLU A 61 13.552 91.627 187.104 1.00 104.40 482 CG GLU A 61 14.214 91.078 188.378 1.00 176.16 483 CD GLU A 61 15.427 91.882 188.853 1.00 198.10 484 OE1 GLU A 61 15.236 93.016 189.341 1.00 190.74 485 OE2 GLU A 61 16.573 91.381 188.747 1.00 185.84 486 C GLU A 61 13.468 91.481 184.602 1.00 72.09 487 O GLU A 61 12.846 90.496 184.214 1.00 44.44 488 N ASP A 62 13.418 92.657 183.987 1.00 43.54 489 CA ASP A 62 12.589 92.874 182.816 1.00 19.32 490 CB ASP A 62 12.312 94.371 182.659 1.00 5.54 491 CG ASP A 62 11.524 94.956 183.850 1.00 95.59 492 OD1 ASP A 62 10.790 94.200 184.540 1.00 64.35 493 OD2 ASP A 62 11.618 96.182 184.091 1.00 64.15 494 C ASP A 62 13.156 92.283 181.519 1.00 28.80 495 O ASP A 62 12.492 92.276 180.483 1.00 23.08 496 N SER A 63 14.378 91.772 181.558 1.00 39.71 497 CA SER A 63 14.940 91.174 180.353 1.00 51.88 498 CB SER A 63 16.395 90.770 180.579 1.00 43.74 499 OG SER A 63 17.214 91.898 180.813 1.00 80.04 500 C SER A 63 14.108 89.938 180.092 1.00 33.07 501 O SER A 63 13.290 89.573 180.919 1.00 42.64 502 N GLY A 64 14.295 89.293 178.949 1.00 33.31 503 CA GLY A 64 13.529 88.085 178.701 1.00 47.82 504 C GLY A 64 12.703 87.912 177.437 1.00 78.77 505 O GLY A 64 12.738 88.718 176.503 1.00 41.30 506 N GLU A 65 11.947 86.819 177.426 1.00 38.56 507 CA GLU A 65 11.096 86.471 176.303 1.00 61.82 508 CB GLU A 65 11.022 84.950 176.157 1.00 56.45 509 CG GLU A 65 9.864 84.452 175.314 1.00 60.09 510 CD GLU A 65 9.860 82.944 175.145 1.00 97.74 511 OE1 GLU A 65 9.816 82.221 176.165 1.00 145.16 512 OE2 GLU A 65 9.898 82.480 173.987 1.00 99.49 513 C GLU A 65 9.693 87.030 176.447 1.00 47.26 514 O GLU A 65 9.000 86.742 177.415 1.00 50.30 515 N TYR A 66 9.282 87.829 175.468 1.00 55.07 516 CA TYR A 66 7.951 88.414 175.462 1.00 29.51 517 CB TYR A 66 8.037 89.931 175.342 1.00 33.26 518 CG TYR A 66 8.495 90.627 176.599 1.00 36.26 519 CD1 TYR A 66 9.844 90.671 176.946 1.00 54.70 520 CE1 TYR A 66 10.264 91.287 178.118 1.00 20.05 521 CD2 TYR A 66 7.574 91.217 177.456 1.00 14.39 522 CE2 TYR A 66 7.978 91.827 178.623 1.00 52.79 523 CZ TYR A 66 9.323 91.862 178.952 1.00 76.87 524 OH TYR A 66 9.709 92.485 180.115 1.00 49.97 525 C TYR A 66 7.135 87.859 174.296 1.00 58.69 526 O TYR A 66 7.653 87.704 173.190 1.00 49.90 527 N LYS A 67 5.866 87.548 174.560 1.00 53.66 528 CA LYS A 67 4.946 87.023 173.550 1.00 38.25 529 CB LYS A 67 4.957 85.504 173.534 1.00 5.42 530 CG LYS A 67 6.054 84.856 172.724 1.00 46.81 531 CD LYS A 67 5.918 83.324 172.794 1.00 100.90 532 CE LYS A 67 5.849 82.829 174.249 1.00 91.92 533 NZ LYS A 67 5.762 81.347 174.372 1.00 45.56 534 C LYS A 67 3.530 87.460 173.867 1.00 67.55 535 O LYS A 67 3.164 87.560 175.038 1.00 52.62 536 N CYS A 68 2.741 87.730 172.830 1.00 27.93 537 CA CYS A 68 1.346 88.113 173.023 1.00 62.04 538 C CYS A 68 0.522 87.234 172.111 1.00 74.23 539 O CYS A 68 0.992 86.816 171.060 1.00 45.57 540 CB CYS A 68 1.092 89.597 172.678 1.00 29.72 541 SG CYS A 68 1.419 90.098 170.952 1.00 99.54 542 N GLN A 69 −0.695 86.920 172.525 1.00 33.27 543 CA GLN A 69 −1.553 86.119 171.681 1.00 50.08 544 CB GLN A 69 −1.489 84.636 172.081 1.00 48.05 545 CG GLN A 69 −2.425 84.215 173.203 1.00 61.10 546 CD GLN A 69 −2.526 82.705 173.318 1.00 71.23 547 OE1 GLN A 69 −2.813 82.023 172.336 1.00 91.00 548 NE2 GLN A 69 −2.294 82.174 174.516 1.00 82.52 549 C GLN A 69 −2.951 86.698 171.837 1.00 82.00 550 O GLN A 69 −3.259 87.275 172.881 1.00 33.84 551 N HIS A 70 −3.780 86.569 170.798 1.00 41.19 552 CA HIS A 70 −5.135 87.114 170.836 1.00 43.14 553 CB HIS A 70 −5.503 87.695 169.484 1.00 74.38 554 CG HIS A 70 −4.758 88.949 169.156 1.00 88.05 555 CD2 HIS A 70 −4.093 89.321 168.038 1.00 38.05 556 ND1 HIS A 70 −4.693 90.022 170.019 1.00 28.06 557 CE1 HIS A 70 −4.025 91.004 169.442 1.00 56.78 558 NE2 HIS A 70 −3.651 90.603 168.240 1.00 58.51 559 C HIS A 70 −6.193 86.125 171.279 1.00 67.91 560 O HIS A 70 −6.224 85.738 172.448 1.00 57.73 561 N GLN A 71 −7.103 85.741 170.393 1.00 57.13 562 CA GLN A 71 −8.074 84.755 170.836 1.00 92.00 563 CB GLN A 71 −9.521 85.291 170.854 1.00 30.07 564 CG GLN A 71 −9.993 86.007 169.632 1.00 41.74 565 CD GLN A 71 −11.225 86.849 169.901 1.00 87.95 566 OE1 GLN A 71 −11.837 86.748 170.965 1.00 35.65 567 NE2 GLN A 71 −11.597 87.690 168.927 1.00 53.82 568 C GLN A 71 −7.944 83.483 170.037 1.00 34.54 569 O GLN A 71 −8.800 82.610 170.102 1.00 84.17 570 N GLN A 72 −6.840 83.376 169.302 1.00 51.65 571 CA GLN A 72 −6.556 82.167 168.543 1.00 53.66 572 CB GLN A 72 −6.029 82.497 167.153 1.00 40.22 573 CG GLN A 72 −7.084 82.254 166.099 1.00 83.83 574 CD GLN A 72 −6.726 82.827 164.759 1.00 29.94 575 OE1 GLN A 72 −5.765 82.397 164.129 1.00 114.76 576 NE2 GLN A 72 −7.500 83.813 164.310 1.00 98.66 577 C GLN A 72 −5.573 81.267 169.288 1.00 43.67 578 O GLN A 72 −5.373 81.404 170.490 1.00 58.65 579 N VAL A 73 −4.958 80.337 168.583 1.00 56.83 580 CA VAL A 73 −4.054 79.418 169.252 1.00 51.40 581 CB VAL A 73 −4.188 77.998 168.669 1.00 106.92 582 CG1 VAL A 73 −3.580 77.944 167.252 1.00 46.73 583 CG2 VAL A 73 −3.536 76.996 169.604 1.00 22.40 584 C VAL A 73 −2.622 79.862 169.121 1.00 64.50 585 O VAL A 73 −1.851 79.805 170.077 1.00 72.42 586 N ALA A 74 −2.270 80.292 167.919 1.00 78.31 587 CA ALA A 74 −0.924 80.744 167.649 1.00 78.26 588 CB ALA A 74 −0.740 80.981 166.166 1.00 125.54 589 C ALA A 74 −0.649 82.019 168.418 1.00 66.03 590 O ALA A 74 −1.553 82.817 168.681 1.00 85.24 591 N GLU A 75 0.616 82.194 168.768 1.00 67.79 592 CA GLU A 75 1.082 83.347 169.516 1.00 53.61 593 CB GLU A 75 1.465 82.908 170.935 1.00 18.85 594 CG GLU A 75 2.031 81.485 170.991 1.00 113.19 595 CD GLU A 75 2.349 81.011 172.398 1.00 127.80 596 OE1 GLU A 75 1.510 81.209 173.305 1.00 114.51 597 OE2 GLU A 75 3.435 80.426 172.593 1.00 173.92 598 C GLU A 75 2.274 83.945 168.773 1.00 48.86 599 O GLU A 75 3.007 83.243 168.075 1.00 57.67 600 N SER A 76 2.445 85.251 168.916 1.00 46.16 601 CA SER A 76 3.520 85.981 168.260 1.00 64.43 602 CB SER A 76 3.619 87.383 168.864 1.00 108.46 603 OG SER A 76 3.634 87.336 170.287 1.00 78.81 604 C SER A 76 4.865 85.291 168.375 1.00 57.59 605 O SER A 76 5.108 84.573 169.339 1.00 53.17 606 N GLU A 77 5.728 85.486 167.379 1.00 95.85 607 CA GLU A 77 7.064 84.906 167.442 1.00 46.97 608 CB GLU A 77 7.893 85.273 166.211 1.00 62.29 609 CG GLU A 77 7.364 84.714 164.896 1.00 130.97 610 CD GLU A 77 7.571 83.215 164.760 1.00 165.99 611 OE1 GLU A 77 8.743 82.773 164.758 1.00 180.77 612 OE2 GLU A 77 6.566 82.477 164.650 1.00 160.47 613 C GLU A 77 7.579 85.645 168.662 1.00 80.10 614 O GLU A 77 7.229 86.804 168.880 1.00 80.13 615 N PRO A 78 8.410 84.999 169.476 1.00 60.47 616 CD PRO A 78 9.153 83.748 169.255 1.00 68.85 617 CA PRO A 78 8.902 85.692 170.661 1.00 58.42 618 CB PRO A 78 9.606 84.583 171.413 1.00 55.27 619 CG PRO A 78 10.270 83.853 170.283 1.00 88.80 620 C PRO A 78 9.836 86.843 170.322 1.00 68.90 621 O PRO A 78 10.461 86.855 169.263 1.00 56.81 622 N VAL A 79 9.914 87.809 171.231 1.00 55.88 623 CA VAL A 79 10.785 88.963 171.075 1.00 53.98 624 CB VAL A 79 9.980 90.251 170.992 1.00 34.06 625 CG1 VAL A 79 10.910 91.426 170.825 1.00 85.73 626 CG2 VAL A 79 9.028 90.171 169.833 1.00 97.73 627 C VAL A 79 11.649 89.009 172.321 1.00 87.70 628 O VAL A 79 11.119 89.113 173.433 1.00 48.94 629 N TYR A 80 12.968 88.928 172.142 1.00 53.61 630 CA TYR A 80 13.878 88.944 173.278 1.00 34.81 631 CB TYR A 80 15.023 87.972 173.020 1.00 65.29 632 CG TYR A 80 14.516 86.557 172.856 1.00 94.10 633 CD1 TYR A 80 14.499 85.938 171.605 1.00 67.48 634 CE1 TYR A 80 13.965 84.657 171.442 1.00 77.57 635 CD2 TYR A 80 13.989 85.856 173.947 1.00 68.38 636 CE2 TYR A 80 13.451 84.578 173.797 1.00 65.53 637 CZ TYR A 80 13.440 83.985 172.542 1.00 93.69 638 OH TYR A 80 12.885 82.733 172.385 1.00 86.31 639 C TYR A 80 14.390 90.337 173.627 1.00 56.78 640 O TYR A 80 14.892 91.069 172.777 1.00 63.63 641 N LEU A 81 14.244 90.689 174.899 1.00 10.90 642 CA LEU A 81 14.628 91.993 175.411 1.00 19.84 643 CB LEU A 81 13.412 92.635 176.068 1.00 16.84 644 CG LEU A 81 13.534 94.104 176.437 1.00 35.65 645 CD1 LEU A 81 13.214 94.911 175.209 1.00 77.33 646 CD2 LEU A 81 12.585 94.468 177.544 1.00 33.43 647 C LEU A 81 15.748 91.903 176.441 1.00 46.78 648 O LEU A 81 15.522 91.419 177.549 1.00 42.71 649 N GLU A 82 16.939 92.393 176.098 1.00 20.80 650 CA GLU A 82 18.070 92.348 177.024 1.00 45.93 651 CB GLU A 82 19.318 91.828 176.307 1.00 24.73 652 CG GLU A 82 19.115 90.473 175.638 1.00 154.76 653 CD GLU A 82 20.294 90.041 174.785 1.00 173.29 654 OE1 GLU A 82 21.395 89.842 175.353 1.00 124.38 655 OE2 GLU A 82 20.112 89.903 173.550 1.00 145.47 656 C GLU A 82 18.361 93.713 177.634 1.00 51.76 657 O GLU A 82 18.443 94.705 176.919 1.00 33.44 658 N VAL A 83 18.514 93.756 178.957 1.00 5.42 659 CA VAL A 83 18.800 95.000 179.663 1.00 45.28 660 CB VAL A 83 17.904 95.144 180.900 1.00 55.93 661 CG1 VAL A 83 18.181 96.457 181.587 1.00 84.34 662 CG2 VAL A 83 16.457 95.065 180.499 1.00 47.82 663 C VAL A 83 20.263 95.031 180.108 1.00 52.84 664 O VAL A 83 20.694 94.195 180.901 1.00 69.13 665 N PHE A 84 21.018 96.007 179.610 1.00 62.21 666 CA PHE A 84 22.439 96.126 179.926 1.00 41.74 667 CB PHE A 84 23.249 96.308 178.653 1.00 33.99 668 CG PHE A 84 23.117 95.196 177.675 1.00 27.72 669 CD1 PHE A 84 21.904 94.910 177.096 1.00 35.75 670 CD2 PHE A 84 24.230 94.459 177.298 1.00 63.18 671 CE1 PHE A 84 21.797 93.908 176.149 1.00 106.48 672 CE2 PHE A 84 24.135 93.457 176.353 1.00 72.91 673 CZ PHE A 84 22.917 93.179 175.776 1.00 70.31 674 C PHE A 84 22.807 97.288 180.825 1.00 50.31 675 O PHE A 84 21.989 98.152 181.116 1.00 51.85 676 N SER A 85 24.075 97.293 181.228 1.00 58.67 677 CA SER A 85 24.676 98.342 182.054 1.00 62.35 678 CB SER A 85 24.515 98.072 183.537 1.00 63.27 679 OG SER A 85 25.416 98.903 184.249 1.00 42.99 680 C SER A 85 26.162 98.412 181.760 1.00 20.41 681 O SER A 85 26.969 97.836 182.480 1.00 71.62 682 N ASP A 86 26.503 99.124 180.694 1.00 57.01 683 CA ASP A 86 27.873 99.290 180.252 1.00 18.49 684 CB ASP A 86 28.179 98.274 179.158 1.00 54.07 685 CG ASP A 86 29.651 98.139 178.883 1.00 94.47 686 OD1 ASP A 86 30.251 99.061 178.284 1.00 107.01 687 OD2 ASP A 86 30.210 97.095 179.277 1.00 121.47 688 C ASP A 86 28.036 100.719 179.739 1.00 38.14 689 O ASP A 86 27.162 101.559 179.934 1.00 28.17 690 N TRP A 87 29.143 101.007 179.080 1.00 27.21 691 CA TRP A 87 29.360 102.359 178.621 1.00 5.42 692 CB TRP A 87 30.850 102.677 178.615 1.00 66.21 693 CG TRP A 87 31.410 102.892 179.971 1.00 5.42 694 CD2 TRP A 87 31.589 104.143 180.619 1.00 22.62 695 CE2 TRP A 87 32.119 103.885 181.897 1.00 32.39 696 CE3 TRP A 87 31.356 105.467 180.243 1.00 27.34 697 CD1 TRP A 87 31.831 101.934 180.863 1.00 80.10 698 NE1 TRP A 87 32.259 102.528 182.026 1.00 27.00 699 CZ2 TRP A 87 32.415 104.901 182.795 1.00 66.07 700 CZ3 TRP A 87 31.650 106.465 181.127 1.00 5.42 701 CH2 TRP A 87 32.174 106.185 182.389 1.00 51.52 702 C TRP A 87 28.756 102.597 177.260 1.00 55.21 703 O TRP A 87 28.120 103.633 177.043 1.00 35.93 704 N LEU A 88 28.962 101.657 176.340 1.00 11.34 705 CA LEU A 88 28.380 101.771 175.005 1.00 32.20 706 CB LEU A 88 29.448 101.985 173.934 1.00 5.42 707 CG LEU A 88 30.149 103.334 174.042 1.00 25.97 708 CD1 LEU A 88 30.908 103.647 172.772 1.00 8.11 709 CD2 LEU A 88 29.107 104.407 174.305 1.00 18.42 710 C LEU A 88 27.579 100.530 174.686 1.00 40.80 711 O LEU A 88 27.996 99.411 174.969 1.00 71.11 712 N LEU A 89 26.413 100.743 174.097 1.00 29.92 713 CA LEU A 89 25.514 99.660 173.727 1.00 40.51 714 CB LEU A 89 24.232 99.746 174.553 1.00 29.28 715 CG LEU A 89 23.183 98.661 174.363 1.00 41.41 716 CD1 LEU A 89 23.364 97.607 175.406 1.00 8.36 717 CD2 LEU A 89 21.807 99.251 174.519 1.00 110.85 718 C LEU A 89 25.186 99.855 172.258 1.00 55.63 719 O LEU A 89 24.869 100.964 171.825 1.00 37.39 720 N LEU A 90 25.293 98.792 171.477 1.00 38.50 721 CA LEU A 90 24.983 98.911 170.063 1.00 17.59 722 CB LEU A 90 25.917 98.066 169.229 1.00 8.86 723 CG LEU A 90 25.566 98.059 167.755 1.00 23.44 724 CD1 LEU A 90 26.146 99.279 167.081 1.00 27.66 725 CD2 LEU A 90 26.117 96.794 167.137 1.00 25.45 726 C LEU A 90 23.587 98.383 169.924 1.00 38.66 727 O LEU A 90 23.330 97.213 170.195 1.00 48.96 728 N GLN A 91 22.681 99.251 169.505 1.00 36.75 729 CA GLN A 91 21.295 98.871 169.354 1.00 8.29 730 CB GLN A 91 20.401 99.929 169.966 1.00 39.59 731 CG GLN A 91 20.488 100.046 171.453 1.00 5.42 732 CD GLN A 91 19.685 101.217 171.942 1.00 54.77 733 OE1 GLN A 91 19.702 102.288 171.325 1.00 27.61 734 NE2 GLN A 91 18.983 101.036 173.053 1.00 32.79 735 C GLN A 91 20.927 98.713 167.903 1.00 57.80 736 O GLN A 91 21.387 99.472 167.049 1.00 61.80 737 N ALA A 92 20.083 97.727 167.624 1.00 41.69 738 CA ALA A 92 19.652 97.509 166.262 1.00 33.39 739 CB ALA A 92 20.287 96.263 165.698 1.00 53.81 740 C ALA A 92 18.147 97.400 166.213 1.00 66.17 741 O ALA A 92 17.518 96.880 167.141 1.00 43.51 742 N SER A 93 17.592 97.919 165.121 1.00 31.27 743 CA SER A 93 16.163 97.913 164.863 1.00 58.56 744 CB SER A 93 15.890 98.616 163.541 1.00 37.57 745 OG SER A 93 16.522 97.916 162.484 1.00 75.71 746 C SER A 93 15.629 96.478 164.810 1.00 81.43 747 O SER A 93 14.493 96.216 165.208 1.00 48.00 748 N ALA A 94 16.454 95.560 164.317 1.00 14.94 749 CA ALA A 94 16.084 94.157 164.218 1.00 54.65 750 CB ALA A 94 15.137 93.958 163.058 1.00 117.54 751 C ALA A 94 17.323 93.302 164.028 1.00 55.96 752 O ALA A 94 18.162 93.613 163.198 1.00 62.00 753 N GLU A 95 17.433 92.214 164.780 1.00 54.57 754 CA GLU A 95 18.605 91.356 164.667 1.00 61.37 755 CB GLU A 95 18.722 90.493 165.917 1.00 82.00 756 CG GLU A 95 18.730 91.321 167.184 1.00 46.60 757 CD GLU A 95 18.734 90.472 168.427 1.00 114.77 758 OE1 GLU A 95 17.813 89.639 168.582 1.00 140.88 759 OE2 GLU A 95 19.659 90.640 169.247 1.00 105.98 760 C GLU A 95 18.598 90.494 163.408 1.00 47.61 761 O GLU A 95 19.650 90.135 162.888 1.00 68.07 762 N VAL A 96 17.407 90.163 162.926 1.00 79.01 763 CA VAL A 96 17.246 89.377 161.703 1.00 53.09 764 CB VAL A 96 16.572 88.026 161.974 1.00 60.34 765 CG1 VAL A 96 16.439 87.269 160.687 1.00 66.62 766 CG2 VAL A 96 17.384 87.219 162.972 1.00 75.27 767 C VAL A 96 16.348 90.214 160.801 1.00 37.17 768 O VAL A 96 15.182 90.453 161.107 1.00 67.51 769 N VAL A 97 16.900 90.673 159.692 1.00 31.53 770 CA VAL A 97 16.164 91.532 158.786 1.00 61.27 771 CB VAL A 97 16.945 92.851 158.561 1.00 37.63 772 CG1 VAL A 97 16.712 93.382 157.165 1.00 101.90 773 CG2 VAL A 97 16.501 93.882 159.579 1.00 109.18 774 C VAL A 97 15.894 90.875 157.450 1.00 74.73 775 O VAL A 97 16.828 90.509 156.745 1.00 91.83 776 N MET A 98 14.615 90.734 157.103 1.00 107.16 777 CA MET A 98 14.229 90.126 155.835 1.00 85.06 778 CB MET A 98 12.701 90.028 155.717 1.00 152.68 779 CG MET A 98 12.042 89.134 156.758 1.00 194.20 780 SD MET A 98 10.239 89.149 156.658 1.00 216.44 781 CE MET A 98 9.857 90.576 157.704 1.00 214.75 782 C MET A 98 14.778 90.978 154.699 1.00 101.32 783 O MET A 98 14.724 92.203 154.747 1.00 54.34 784 N GLU A 99 15.315 90.312 153.684 1.00 129.05 785 CA GLU A 99 15.895 90.956 152.506 1.00 108.86 786 CB GLU A 99 15.975 89.918 151.373 1.00 189.93 787 CG GLU A 99 16.759 90.309 150.123 1.00 203.35 788 CD GLU A 99 16.928 89.132 149.164 1.00 206.77 789 OE1 GLU A 99 15.908 88.496 148.810 1.00 194.67 790 OE2 GLU A 99 18.079 88.844 148.765 1.00 186.48 791 C GLU A 99 15.083 92.177 152.061 1.00 72.06 792 O GLU A 99 13.856 92.132 152.005 1.00 110.93 793 N GLY A 100 15.770 93.271 151.758 1.00 62.36 794 CA GLY A 100 15.080 94.470 151.312 1.00 77.49 795 C GLY A 100 14.648 95.464 152.380 1.00 106.99 796 O GLY A 100 14.773 96.675 152.180 1.00 142.90 797 N GLN A 101 14.134 94.967 153.505 1.00 76.10 798 CA GLN A 101 13.691 95.830 154.606 1.00 99.54 799 CB GLN A 101 13.125 94.970 155.749 1.00 118.17 800 CG GLN A 101 11.942 94.075 155.371 1.00 127.37 801 CD GLN A 101 10.670 94.847 155.045 1.00 143.15 802 OE1 GLN A 101 10.628 96.072 155.148 1.00 128.68 803 NE2 GLN A 101 9.622 94.125 154.657 1.00 171.66 804 C GLN A 101 14.821 96.737 155.149 1.00 80.68 805 O GLN A 101 16.007 96.446 154.978 1.00 81.82 806 N PRO A 102 14.461 97.854 155.803 1.00 39.03 807 CD PRO A 102 13.105 98.404 155.959 1.00 80.04 808 CA PRO A 102 15.446 98.779 156.359 1.00 46.08 809 CB PRO A 102 14.633 100.039 156.586 1.00 68.48 810 CG PRO A 102 13.316 99.493 156.982 1.00 39.46 811 C PRO A 102 16.106 98.283 157.645 1.00 68.21 812 O PRO A 102 15.560 97.432 158.365 1.00 33.76 813 N LEU A 103 17.280 98.847 157.924 1.00 47.86 814 CA LEU A 103 18.070 98.496 159.093 1.00 42.26 815 CB LEU A 103 19.201 97.587 158.673 1.00 5.42 816 CG LEU A 103 20.077 97.146 159.825 1.00 53.71 817 CD1 LEU A 103 19.245 96.340 160.809 1.00 30.09 818 CD2 LEU A 103 21.239 96.342 159.271 1.00 40.52 819 C LEU A 103 18.656 99.713 159.791 1.00 39.88 820 O LEU A 103 19.091 100.667 159.149 1.00 48.87 821 N PHE A 104 18.690 99.675 161.113 1.00 16.90 822 CA PHE A 104 19.229 100.796 161.853 1.00 47.53 823 CB PHE A 104 18.107 101.655 162.406 1.00 17.73 824 CG PHE A 104 17.195 102.171 161.361 1.00 55.90 825 CD1 PHE A 104 15.965 101.566 161.139 1.00 15.89 826 CD2 PHE A 104 17.569 103.257 160.577 1.00 76.37 827 CE1 PHE A 104 15.105 102.040 160.146 1.00 68.24 828 CE2 PHE A 104 16.719 103.743 159.579 1.00 94.38 829 CZ PHE A 104 15.481 103.133 159.363 1.00 50.60 830 C PHE A 104 20.150 100.419 162.978 1.00 42.37 831 O PHE A 104 19.834 99.593 163.832 1.00 47.93 832 N LEU A 105 21.306 101.049 162.970 1.00 26.80 833 CA LEU A 105 22.277 100.811 163.995 1.00 33.05 834 CB LEU A 105 23.609 100.437 163.362 1.00 47.90 835 CG LEU A 105 23.596 99.200 162.464 1.00 47.60 836 CD1 LEU A 105 24.941 99.044 161.777 1.00 83.01 837 CD2 LEU A 105 23.285 97.976 163.291 1.00 13.75 838 C LEU A 105 22.391 102.129 164.720 1.00 52.31 839 O LEU A 105 22.230 103.192 164.123 1.00 53.94 840 N ARG A 106 22.676 102.055 166.010 1.00 21.83 841 CA ARG A 106 22.819 103.239 166.837 1.00 41.63 842 CB ARG A 106 21.456 103.568 167.438 1.00 23.32 843 CG ARG A 106 21.448 104.739 168.369 1.00 51.86 844 CD ARG A 106 20.098 104.857 169.030 1.00 30.81 845 NE ARG A 106 20.162 105.533 170.318 1.00 31.36 846 CZ ARG A 106 19.100 105.803 171.065 1.00 52.13 847 NH1 ARG A 106 17.892 105.459 170.642 1.00 93.33 848 NH2 ARG A 106 19.240 106.401 172.241 1.00 34.31 849 C ARG A 106 23.838 102.977 167.956 1.00 57.42 850 O ARG A 106 23.716 101.991 168.685 1.00 30.30 851 N CYS A 107 24.866 103.815 168.077 1.00 24.37 852 CA CYS A 107 25.807 103.616 169.176 1.00 42.73 853 C CYS A 107 25.176 104.464 170.251 1.00 44.66 854 O CYS A 107 25.065 105.682 170.102 1.00 52.70 855 CB CYS A 107 27.216 104.119 168.858 1.00 5.42 856 SG CYS A 107 28.525 103.331 169.872 1.00 82.53 857 N HIS A 108 24.717 103.804 171.311 1.00 11.14 858 CA HIS A 108 24.045 104.487 172.398 1.00 21.95 859 CB HIS A 108 22.770 103.755 172.765 1.00 13.74 860 CG HIS A 108 21.954 104.478 173.783 1.00 50.61 861 CD2 HIS A 108 21.270 104.037 174.864 1.00 13.51 862 ND1 HIS A 108 21.783 105.845 173.750 1.00 39.22 863 CE1 HIS A 108 21.030 106.213 174.769 1.00 67.80 864 NE2 HIS A 108 20.706 105.135 175.460 1.00 46.62 865 C HIS A 108 24.898 104.633 173.634 1.00 52.09 866 O HIS A 108 25.330 103.648 174.220 1.00 15.69 867 N GLY A 109 25.122 105.874 174.047 1.00 37.30 868 CA GLY A 109 25.950 106.085 175.212 1.00 36.86 869 C GLY A 109 25.165 106.142 176.498 1.00 46.50 870 O GLY A 109 24.159 106.838 176.579 1.00 42.12 871 N TRP A 110 25.641 105.412 177.501 1.00 7.94 872 CA TRP A 110 25.033 105.365 178.824 1.00 30.83 873 CB TRP A 110 26.075 104.901 179.816 1.00 5.42 874 CG TRP A 110 25.536 104.902 181.182 1.00 67.67 875 CD2 TRP A 110 24.735 103.879 181.772 1.00 56.37 876 CE2 TRP A 110 24.444 104.283 183.085 1.00 18.12 877 CE3 TRP A 110 24.239 102.654 181.316 1.00 81.28 878 CD1 TRP A 110 25.692 105.866 182.129 1.00 37.15 879 NE1 TRP A 110 25.039 105.500 183.283 1.00 90.09 880 CZ2 TRP A 110 23.685 103.510 183.944 1.00 53.89 881 CZ3 TRP A 110 23.484 101.886 182.176 1.00 86.79 882 CH2 TRP A 110 23.216 102.317 183.476 1.00 35.12 883 C TRP A 110 24.430 106.697 179.304 1.00 25.46 884 O TRP A 110 24.984 107.758 179.042 1.00 34.32 885 N ARG A 111 23.324 106.639 180.045 1.00 9.65 886 CA ARG A 111 22.640 107.855 180.509 1.00 64.56 887 CB ARG A 111 23.299 108.434 181.778 1.00 5.57 888 CG ARG A 111 23.045 107.558 183.026 1.00 122.90 889 CD ARG A 111 23.274 108.250 184.384 1.00 92.09 890 NE ARG A 111 22.026 108.704 185.001 1.00 66.00 891 CZ ARG A 111 21.283 109.706 184.540 1.00 111.74 892 NH1 ARG A 111 21.659 110.370 183.454 1.00 85.41 893 NH2 ARG A 111 20.159 110.045 185.159 1.00 106.66 894 C ARG A 111 22.590 108.889 179.383 1.00 25.39 895 O ARG A 111 22.455 110.096 179.584 1.00 35.74 896 N ASN A 112 22.668 108.367 178.176 1.00 22.55 897 CA ASN A 112 22.638 109.160 176.979 1.00 55.36 898 CB ASN A 112 21.259 109.811 176.809 1.00 23.18 899 CG ASN A 112 20.903 110.048 175.338 1.00 99.46 900 OD1 ASN A 112 21.105 109.180 174.484 1.00 76.98 901 ND2 ASN A 112 20.363 111.225 175.042 1.00 120.92 902 C ASN A 112 23.759 110.186 177.006 1.00 30.60 903 O ASN A 112 23.623 111.301 176.503 1.00 78.43 904 N TRP A 113 24.884 109.793 177.590 1.00 28.24 905 CA TRP A 113 26.034 110.674 177.632 1.00 46.75 906 CB TRP A 113 27.127 110.128 178.532 1.00 19.32 907 CG TRP A 113 26.882 110.334 179.969 1.00 11.92 908 CD2 TRP A 113 27.516 109.646 181.050 1.00 26.29 909 CE2 TRP A 113 27.000 110.174 182.242 1.00 5.42 910 CE3 TRP A 113 28.477 108.636 181.124 1.00 22.82 911 CD1 TRP A 113 26.037 111.226 180.528 1.00 35.81 912 NE1 TRP A 113 26.095 111.138 181.899 1.00 39.35 913 CZ2 TRP A 113 27.411 109.724 183.501 1.00 42.09 914 CZ3 TRP A 113 28.886 108.191 182.375 1.00 13.91 915 CH2 TRP A 113 28.355 108.733 183.542 1.00 5.42 916 C TRP A 113 26.585 110.818 176.232 1.00 39.58 917 O TRP A 113 26.479 109.921 175.397 1.00 56.66 918 N ASP A 114 27.174 111.970 175.983 1.00 40.70 919 CA ASP A 114 27.749 112.254 174.696 1.00 44.29 920 CB ASP A 114 28.223 113.698 174.678 1.00 49.96 921 CG ASP A 114 27.094 114.663 174.860 1.00 31.77 922 OD1 ASP A 114 26.224 114.722 173.964 1.00 75.41 923 OD2 ASP A 114 27.072 115.349 175.897 1.00 54.49 924 C ASP A 114 28.910 111.324 174.393 1.00 58.03 925 O ASP A 114 29.718 111.023 175.268 1.00 34.68 926 N VAL A 115 28.967 110.858 173.148 1.00 30.06 927 CA VAL A 115 30.048 109.990 172.687 1.00 31.75 928 CB VAL A 115 29.579 108.551 172.316 1.00 9.73 929 CG1 VAL A 115 30.611 107.900 171.442 1.00 60.47 930 CG2 VAL A 115 29.447 107.693 173.535 1.00 5.42 931 C VAL A 115 30.623 110.612 171.426 1.00 24.47 932 O VAL A 115 29.931 110.735 170.423 1.00 47.65 933 N TYR A 116 31.886 111.012 171.465 1.00 30.10 934 CA TYR A 116 32.479 111.602 170.279 1.00 17.95 935 CB TYR A 116 33.256 112.865 170.637 1.00 61.65 936 CG TYR A 116 32.427 113.950 171.286 1.00 16.29 937 CD1 TYR A 116 32.051 113.862 172.611 1.00 20.60 938 CE1 TYR A 116 31.273 114.839 173.205 1.00 49.07 939 CD2 TYR A 116 32.004 115.049 170.560 1.00 22.42 940 CE2 TYR A 116 31.227 116.031 171.138 1.00 73.73 941 CZ TYR A 116 30.864 115.920 172.460 1.00 14.21 942 OH TYR A 116 30.091 116.898 173.033 1.00 94.60 943 C TYR A 116 33.391 110.599 169.588 1.00 45.63 944 O TYR A 116 33.850 109.628 170.205 1.00 28.02 945 N LYS A 117 33.636 110.842 168.302 1.00 6.49 946 CA LYS A 117 34.479 109.975 167.479 1.00 35.81 947 CB LYS A 117 35.937 110.034 167.974 1.00 21.69 948 CG LYS A 117 36.715 111.214 167.404 1.00 9.02 949 CD LYS A 117 37.800 111.699 168.323 1.00 36.98 950 CE LYS A 117 38.449 112.977 167.779 1.00 25.36 951 NZ LYS A 117 39.653 113.406 168.569 1.00 25.77 952 C LYS A 117 33.962 108.543 167.472 1.00 7.50 953 O LYS A 117 34.687 107.595 167.749 1.00 52.96 954 N VAL A 118 32.693 108.398 167.136 1.00 46.87 955 CA VAL A 118 32.045 107.102 167.109 1.00 14.75 956 CB VAL A 118 30.540 107.259 167.103 1.00 8.67 957 CG1 VAL A 118 29.897 105.947 167.298 1.00 27.58 958 CG2 VAL A 118 30.122 108.227 168.165 1.00 69.02 959 C VAL A 118 32.404 106.398 165.829 1.00 30.61 960 O VAL A 118 32.314 106.981 164.755 1.00 19.62 961 N ILE A 119 32.821 105.148 165.939 1.00 26.47 962 CA ILE A 119 33.130 104.369 164.753 1.00 43.90 963 CB ILE A 119 34.604 104.042 164.634 1.00 35.19 964 CG2 ILE A 119 34.809 103.093 163.482 1.00 23.28 965 CG1 ILE A 119 35.406 105.305 164.379 1.00 48.21 966 CD1 ILE A 119 36.855 105.042 164.194 1.00 13.69 967 C ILE A 119 32.391 103.054 164.815 1.00 59.19 968 O ILE A 119 32.403 102.371 165.840 1.00 67.21 969 N TYR A 120 31.743 102.698 163.720 1.00 17.08 970 CA TYR A 120 31.023 101.445 163.679 1.00 30.07 971 CB TYR A 120 29.692 101.622 162.976 1.00 13.53 972 CG TYR A 120 28.673 102.393 163.755 1.00 11.12 973 CD1 TYR A 120 28.517 103.760 163.585 1.00 17.26 974 CE1 TYR A 120 27.509 104.438 164.227 1.00 5.42 975 CD2 TYR A 120 27.806 101.737 164.599 1.00 25.25 976 CE2 TYR A 120 26.803 102.398 165.243 1.00 15.18 977 CZ TYR A 120 26.647 103.740 165.056 1.00 46.64 978 OH TYR A 120 25.595 104.357 165.687 1.00 52.40 979 C TYR A 120 31.864 100.435 162.917 1.00 68.41 980 O TYR A 120 32.395 100.743 161.850 1.00 28.49 981 N TYR A 121 31.991 99.229 163.466 1.00 51.87 982 CA TYR A 121 32.769 98.187 162.811 1.00 25.77 983 CB TYR A 121 33.826 97.598 163.747 1.00 54.55 984 CG TYR A 121 34.978 98.529 164.015 1.00 8.44 985 CD1 TYR A 121 34.991 99.343 165.133 1.00 59.81 986 CE1 TYR A 121 36.010 100.254 165.343 1.00 105.65 987 CD2 TYR A 121 36.022 98.645 163.112 1.00 79.41 988 CE2 TYR A 121 37.047 99.558 163.313 1.00 65.81 989 CZ TYR A 121 37.031 100.355 164.426 1.00 13.26 990 OH TYR A 121 38.023 101.270 164.627 1.00 74.37 991 C TYR A 121 31.882 97.078 162.315 1.00 71.36 992 O TYR A 121 30.877 96.730 162.942 1.00 47.92 993 N LYS A 122 32.271 96.533 161.171 1.00 48.07 994 CA LYS A 122 31.550 95.452 160.537 1.00 62.27 995 CB LYS A 122 30.826 95.951 159.290 1.00 82.65 996 CG LYS A 122 30.100 94.878 158.498 1.00 56.59 997 CD LYS A 122 29.471 95.512 157.272 1.00 114.33 998 CE LYS A 122 28.714 94.519 156.423 1.00 90.73 999 NZ LYS A 122 28.074 95.227 155.275 1.00 102.70 1000 C LYS A 122 32.575 94.415 160.149 1.00 51.78 1001 O LYS A 122 33.377 94.622 159.236 1.00 58.80 1002 N ASP A 123 32.544 93.296 160.855 1.00 69.12 1003 CA ASP A 123 33.464 92.205 160.595 1.00 94.48 1004 CB ASP A 123 33.175 91.559 159.230 1.00 102.02 1005 CG ASP A 123 31.808 90.890 159.170 1.00 106.91 1006 OD1 ASP A 123 31.492 90.097 160.087 1.00 80.34 1007 OD2 ASP A 123 31.056 91.152 158.201 1.00 91.23 1008 C ASP A 123 34.887 92.725 160.633 1.00 42.69 1009 O ASP A 123 35.642 92.572 159.682 1.00 80.39 1010 N GLY A 124 35.240 93.353 161.741 1.00 42.82 1011 CA GLY A 124 36.585 93.862 161.892 1.00 58.87 1012 C GLY A 124 36.987 94.991 160.970 1.00 46.57 1013 O GLY A 124 38.117 95.452 161.037 1.00 81.66 1014 N GLU A 125 36.092 95.440 160.102 1.00 57.50 1015 CA GLU A 125 36.434 96.544 159.211 1.00 57.91 1016 CB GLU A 125 35.933 96.298 157.791 1.00 140.86 1017 CG GLU A 125 36.385 95.024 157.122 1.00 176.84 1018 CD GLU A 125 35.928 94.972 155.677 1.00 189.28 1019 OE1 GLU A 125 34.704 95.097 155.438 1.00 165.09 1020 OE2 GLU A 125 36.794 94.814 154.785 1.00 176.42 1021 C GLU A 125 35.779 97.823 159.701 1.00 49.34 1022 O GLU A 125 34.723 97.791 160.328 1.00 70.32 1023 N ALA A 126 36.400 98.953 159.400 1.00 54.71 1024 CA ALA A 126 35.850 100.237 159.793 1.00 36.67 1025 CB ALA A 126 36.928 101.281 159.793 1.00 40.73 1026 C ALA A 126 34.775 100.614 158.799 1.00 28.44 1027 O ALA A 126 35.074 100.962 157.660 1.00 49.69 1028 N LEU A 127 33.523 100.557 159.235 1.00 38.11 1029 CA LEU A 127 32.412 100.888 158.365 1.00 35.41 1030 CB LEU A 127 31.141 100.219 158.880 1.00 24.22 1031 CG LEU A 127 29.869 100.320 158.045 1.00 33.49 1032 CD1 LEU A 127 30.194 100.562 156.587 1.00 56.43 1033 CD2 LEU A 127 29.077 99.041 158.237 1.00 47.01 1034 C LEU A 127 32.226 102.393 158.225 1.00 30.36 1035 O LEU A 127 32.289 102.902 157.118 1.00 60.67 1036 N LYS A 128 32.014 103.108 159.331 1.00 28.99 1037 CA LYS A 128 31.836 104.566 159.273 1.00 33.91 1038 CB LYS A 128 30.366 104.916 159.041 1.00 38.64 1039 CG LYS A 128 30.131 106.337 158.560 1.00 15.25 1040 CD LYS A 128 28.691 106.479 158.073 1.00 113.62 1041 CE LYS A 128 28.493 107.706 157.188 1.00 123.73 1042 NZ LYS A 128 27.202 107.663 156.419 1.00 121.55 1043 C LYS A 128 32.317 105.281 160.530 1.00 52.08 1044 O LYS A 128 32.077 104.819 161.647 1.00 65.58 1045 N TYR A 129 33.011 106.401 160.343 1.00 31.59 1046 CA TYR A 129 33.509 107.213 161.459 1.00 36.12 1047 CB TYR A 129 35.037 107.317 161.450 1.00 18.41 1048 CG TYR A 129 35.608 108.593 162.076 1.00 5.42 1049 CD1 TYR A 129 36.136 108.584 163.348 1.00 44.66 1050 CE1 TYR A 129 36.655 109.734 163.923 1.00 33.53 1051 CD2 TYR A 129 35.619 109.804 161.386 1.00 23.01 1052 CE2 TYR A 129 36.141 110.962 161.959 1.00 5.42 1053 CZ TYR A 129 36.653 110.910 163.229 1.00 39.44 1054 OH TYR A 129 37.173 112.024 163.828 1.00 26.10 1055 C TYR A 129 32.942 108.600 161.285 1.00 49.76 1056 O TYR A 129 32.749 109.063 160.160 1.00 59.27 1057 N TRP A 130 32.696 109.263 162.401 1.00 24.05 1058 CA TRP A 130 32.177 110.612 162.378 1.00 29.33 1059 CB TRP A 130 30.653 110.586 162.363 1.00 41.56 1060 CG TRP A 130 30.067 111.918 162.139 1.00 34.89 1061 CD2 TRP A 130 30.311 112.772 161.028 1.00 20.74 1062 CE2 TRP A 130 29.535 113.931 161.210 1.00 30.33 1063 CE3 TRP A 130 31.109 112.673 159.893 1.00 40.31 1064 CD1 TRP A 130 29.177 112.571 162.937 1.00 110.45 1065 NE1 TRP A 130 28.849 113.786 162.385 1.00 102.78 1066 CZ2 TRP A 130 29.540 114.979 160.298 1.00 108.00 1067 CZ3 TRP A 130 31.112 113.715 158.989 1.00 14.76 1068 CH2 TRP A 130 30.337 114.847 159.193 1.00 47.04 1069 C TRP A 130 32.700 111.316 163.628 1.00 59.29 1070 O TRP A 130 32.949 110.683 164.672 1.00 22.78 1071 N TYR A 131 32.875 112.625 163.529 1.00 5.42 1072 CA TYR A 131 33.406 113.361 164.664 1.00 43.44 1073 CB TYR A 131 33.533 114.856 164.336 1.00 20.56 1074 CG TYR A 131 34.068 115.149 162.945 1.00 6.92 1075 CD1 TYR A 131 33.219 115.167 161.850 1.00 40.67 1076 CE1 TYR A 131 33.693 115.445 160.573 1.00 38.77 1077 CD2 TYR A 131 35.422 115.414 162.728 1.00 31.32 1078 CE2 TYR A 131 35.908 115.689 161.455 1.00 16.93 1079 CZ TYR A 131 35.034 115.708 160.384 1.00 49.10 1080 OH TYR A 131 35.486 116.022 159.126 1.00 47.13 1081 C TYR A 131 32.535 113.175 165.887 1.00 28.76 1082 O TYR A 131 33.030 113.124 167.015 1.00 36.69 1083 N GLU A 132 31.232 113.060 165.646 1.00 21.77 1084 CA GLU A 132 30.249 112.914 166.710 1.00 35.07 1085 CB GLU A 132 29.315 114.113 166.691 1.00 5.42 1086 CG GLU A 132 29.974 115.382 167.187 1.00 32.08 1087 CD GLU A 132 30.190 116.404 166.099 1.00 77.18 1088 OE1 GLU A 132 29.797 116.117 164.946 1.00 30.77 1089 OE2 GLU A 132 30.748 117.487 166.408 1.00 46.31 1090 C GLU A 132 29.443 111.640 166.590 1.00 26.10 1091 O GLU A 132 29.647 110.866 165.680 1.00 44.94 1092 N ASN A 133 28.529 111.413 167.518 1.00 42.20 1093 CA ASN A 133 27.708 110.215 167.468 1.00 5.42 1094 CB ASN A 133 26.848 110.093 168.700 1.00 21.79 1095 CG ASN A 133 26.554 108.677 169.032 1.00 28.76 1096 OD1 ASN A 133 26.285 107.878 168.144 1.00 22.35 1097 ND2 ASN A 133 26.603 108.344 170.318 1.00 74.20 1098 C ASN A 133 26.811 110.371 166.285 1.00 11.75 1099 O ASN A 133 26.539 111.500 165.877 1.00 33.27 1100 N HIS A 134 26.338 109.252 165.744 1.00 5.42 1101 CA HIS A 134 25.485 109.278 164.559 1.00 30.76 1102 CB HIS A 134 26.317 109.594 163.321 1.00 50.57 1103 CG HIS A 134 27.435 108.627 163.085 1.00 21.60 1104 CD2 HIS A 134 27.659 107.753 162.077 1.00 76.57 1105 ND1 HIS A 134 28.481 108.468 163.965 1.00 61.39 1106 CE1 HIS A 134 29.300 107.539 163.512 1.00 26.75 1107 NE2 HIS A 134 28.823 107.088 162.368 1.00 47.66 1108 C HIS A 134 24.864 107.917 164.384 1.00 24.80 1109 O HIS A 134 25.441 106.932 164.821 1.00 42.22 1110 N ALA A 135 23.706 107.844 163.733 1.00 51.38 1111 CA ALA A 135 23.053 106.550 163.541 1.00 50.85 1112 CB ALA A 135 21.551 106.694 163.647 1.00 25.54 1113 C ALA A 135 23.428 106.009 162.188 1.00 30.29 1114 O ALA A 135 23.718 106.776 161.277 1.00 75.67 1115 N ILE A 136 23.448 104.687 162.064 1.00 48.62 1116 CA ILE A 136 23.789 104.039 160.802 1.00 34.81 1117 CB ILE A 136 24.593 102.724 160.998 1.00 59.15 1118 CG2 ILE A 136 24.856 102.076 159.664 1.00 5.42 1119 CG1 ILE A 136 25.942 103.004 161.664 1.00 55.26 1120 CD1 ILE A 136 26.878 103.861 160.822 1.00 92.37 1121 C ILE A 136 22.450 103.677 160.245 1.00 36.44 1122 O ILE A 136 21.735 102.876 160.844 1.00 40.66 1123 N SER A 137 22.104 104.274 159.110 1.00 71.47 1124 CA SER A 137 20.813 104.022 158.477 1.00 77.26 1125 CB SER A 137 20.064 105.335 158.248 1.00 65.71 1126 OG SER A 137 19.920 106.070 159.449 1.00 92.34 1127 C SER A 137 20.952 103.301 157.150 1.00 55.90 1128 O SER A 137 21.323 103.895 156.137 1.00 68.68 1129 N ILE A 138 20.650 102.012 157.164 1.00 62.52 1130 CA ILE A 138 20.717 101.202 155.961 1.00 61.92 1131 CB ILE A 138 21.275 99.827 156.270 1.00 45.81 1132 CG2 ILE A 138 21.312 98.999 155.015 1.00 82.72 1133 CG1 ILE A 138 22.673 99.965 156.863 1.00 76.93 1134 CD1 ILE A 138 23.230 98.666 157.415 1.00 63.77 1135 C ILE A 138 19.312 101.056 155.375 1.00 89.17 1136 O ILE A 138 18.525 100.208 155.807 1.00 38.61 1137 N THR A 139 19.023 101.907 154.393 1.00 109.71 1138 CA THR A 139 17.742 101.970 153.689 1.00 95.12 1139 CB THR A 139 17.840 102.956 152.539 1.00 101.48 1140 OG1 THR A 139 19.147 102.850 151.946 1.00 113.46 1141 CG2 THR A 139 17.596 104.370 153.036 1.00 70.63 1142 C THR A 139 17.208 100.663 153.123 1.00 107.81 1143 O THR A 139 16.044 100.321 153.342 1.00 75.17 1144 N ASN A 140 18.048 99.955 152.370 1.00 119.96 1145 CA ASN A 140 17.660 98.679 151.769 1.00 77.07 1146 CB ASN A 140 17.495 98.828 150.257 1.00 128.43 1147 CG ASN A 140 16.465 99.873 149.888 1.00 149.94 1148 OD1 ASN A 140 15.330 99.840 150.365 1.00 158.03 1149 ND2 ASN A 140 16.855 100.810 149.029 1.00 147.94 1150 C ASN A 140 18.691 97.603 152.065 1.00 96.65 1151 O ASN A 140 19.802 97.615 151.527 1.00 86.22 1152 N ALA A 141 18.308 96.666 152.922 1.00 38.12 1153 CA ALA A 141 19.196 95.588 153.316 1.00 94.25 1154 CB ALA A 141 18.435 94.592 154.164 1.00 53.34 1155 C ALA A 141 19.844 94.885 152.126 1.00 79.54 1156 O ALA A 141 19.409 95.042 150.987 1.00 77.48 1157 N ALA A 142 20.889 94.112 152.406 1.00 90.86 1158 CA ALA A 142 21.617 93.374 151.383 1.00 76.61 1159 CB ALA A 142 22.683 94.261 150.761 1.00 121.64 1160 C ALA A 142 22.260 92.150 152.022 1.00 74.42 1161 O ALA A 142 21.987 91.843 153.176 1.00 111.57 1162 N VAL A 143 23.114 91.458 151.274 1.00 108.94 1163 CA VAL A 143 23.795 90.262 151.768 1.00 116.05 1164 CB VAL A 143 24.071 89.259 150.609 1.00 186.06 1165 CG1 VAL A 143 24.745 89.977 149.434 1.00 191.15 1166 CG2 VAL A 143 24.948 88.112 151.109 1.00 210.48 1167 C VAL A 143 25.115 90.625 152.440 1.00 117.36 1168 O VAL A 143 25.496 90.038 153.456 1.00 94.53 1169 N GLU A 144 25.813 91.588 151.853 1.00 118.63 1170 CA GLU A 144 27.080 92.049 152.389 1.00 89.21 1171 CB GLU A 144 27.662 93.116 151.474 1.00 107.26 1172 CG GLU A 144 26.646 94.190 151.126 1.00 114.43 1173 CD GLU A 144 27.276 95.427 150.535 1.00 150.22 1174 OE1 GLU A 144 28.027 95.290 149.546 1.00 173.95 1175 OE2 GLU A 144 27.015 96.535 151.056 1.00 124.46 1176 C GLU A 144 26.810 92.655 153.756 1.00 100.45 1177 O GLU A 144 27.642 92.564 154.661 1.00 113.43 1178 N ASP A 145 25.635 93.269 153.891 1.00 69.60 1179 CA ASP A 145 25.231 93.912 155.135 1.00 62.50 1180 CB ASP A 145 23.927 94.699 154.945 1.00 35.86 1181 CG ASP A 145 24.153 96.053 154.284 1.00 114.94 1182 OD1 ASP A 145 25.187 96.694 154.585 1.00 110.06 1183 OD2 ASP A 145 23.295 96.481 153.477 1.00 95.06 1184 C ASP A 145 25.102 93.000 156.350 1.00 52.48 1185 O ASP A 145 24.774 93.466 157.435 1.00 45.00 1186 N SER A 146 25.339 91.706 156.189 1.00 41.79 1187 CA SER A 146 25.277 90.834 157.347 1.00 56.05 1188 CB SER A 146 24.848 89.426 156.965 1.00 71.16 1189 OG SER A 146 23.440 89.341 156.889 1.00 94.99 1190 C SER A 146 26.658 90.785 157.969 1.00 69.92 1191 O SER A 146 27.594 91.438 157.498 1.00 69.56 1192 N GLY A 147 26.787 90.000 159.026 1.00 47.55 1193 CA GLY A 147 28.067 89.894 159.693 1.00 98.06 1194 C GLY A 147 27.921 90.473 161.076 1.00 50.55 1195 O GLY A 147 26.837 90.915 161.439 1.00 81.86 1196 N THR A 148 28.996 90.477 161.852 1.00 54.75 1197 CA THR A 148 28.923 91.009 163.199 1.00 47.04 1198 CB THR A 148 29.784 90.196 164.160 1.00 5.42 1199 OG1 THR A 148 31.016 90.882 164.383 1.00 70.34 1200 CG2 THR A 148 30.080 88.841 163.572 1.00 60.94 1201 C THR A 148 29.380 92.461 163.255 1.00 42.31 1202 O THR A 148 30.388 92.827 162.656 1.00 52.98 1203 N TYR A 149 28.623 93.285 163.976 1.00 52.62 1204 CA TYR A 149 28.950 94.695 164.128 1.00 25.73 1205 CB TYR A 149 27.786 95.584 163.725 1.00 15.90 1206 CG TYR A 149 27.380 95.588 162.288 1.00 26.25 1207 CD1 TYR A 149 26.653 94.538 161.750 1.00 26.15 1208 CE1 TYR A 149 26.201 94.583 160.445 1.00 48.47 1209 CD2 TYR A 149 27.651 96.686 161.482 1.00 25.17 1210 CE2 TYR A 149 27.206 96.742 160.182 1.00 41.99 1211 CZ TYR A 149 26.483 95.688 159.666 1.00 45.90 1212 OH TYR A 149 26.063 95.738 158.359 1.00 54.85 1213 C TYR A 149 29.266 95.050 165.577 1.00 59.07 1214 O TYR A 149 29.000 94.275 166.503 1.00 29.97 1215 N TYR A 150 29.820 96.244 165.757 1.00 27.86 1216 CA TYR A 150 30.127 96.766 167.078 1.00 46.90 1217 CB TYR A 150 31.126 95.863 167.799 1.00 32.05 1218 CG TYR A 150 32.540 95.971 167.323 1.00 33.00 1219 CD1 TYR A 150 33.391 96.933 167.837 1.00 32.03 1220 CE1 TYR A 150 34.704 97.018 167.419 1.00 59.03 1221 CD2 TYR A 150 33.038 95.093 166.369 1.00 75.94 1222 CE2 TYR A 150 34.349 95.169 165.943 1.00 69.80 1223 CZ TYR A 150 35.177 96.135 166.473 1.00 46.28 1224 OH TYR A 150 36.476 96.223 166.049 1.00 71.42 1225 C TYR A 150 30.667 98.182 166.902 1.00 52.29 1226 O TYR A 150 31.175 98.516 165.836 1.00 49.86 1227 N CYS A 151 30.517 99.025 167.923 1.00 31.32 1228 CA CYS A 151 30.989 100.393 167.832 1.00 7.95 1229 C CYS A 151 31.968 100.769 168.914 1.00 40.57 1230 O CYS A 151 32.057 100.120 169.946 1.00 51.30 1231 CB CYS A 151 29.813 101.372 167.856 1.00 53.04 1232 SG CYS A 151 28.694 101.368 169.294 1.00 69.58 1233 N THR A 152 32.708 101.835 168.663 1.00 26.38 1234 CA THR A 152 33.671 102.341 169.617 1.00 14.07 1235 CB THR A 152 35.085 102.028 169.185 1.00 22.97 1236 OG1 THR A 152 35.335 102.632 167.916 1.00 43.42 1237 CG2 THR A 152 35.276 100.549 169.055 1.00 54.46 1238 C THR A 152 33.489 103.840 169.620 1.00 59.80 1239 O THR A 152 32.993 104.417 168.645 1.00 26.00 1240 N GLY A 153 33.890 104.471 170.715 1.00 24.03 1241 CA GLY A 153 33.751 105.909 170.812 1.00 38.00 1242 C GLY A 153 34.368 106.444 172.082 1.00 50.23 1243 O GLY A 153 34.734 105.680 172.984 1.00 10.68 1244 N LYS A 154 34.497 107.762 172.155 1.00 20.76 1245 CA LYS A 154 35.071 108.364 173.336 1.00 22.57 1246 CB LYS A 154 36.150 109.375 172.947 1.00 18.43 1247 CG LYS A 154 37.401 108.744 172.357 1.00 68.32 1248 CD LYS A 154 38.459 109.762 171.955 1.00 79.74 1249 CE LYS A 154 39.759 109.070 171.557 1.00 96.73 1250 NZ LYS A 154 40.839 110.040 171.221 1.00 103.77 1251 C LYS A 154 33.937 109.023 174.095 1.00 49.37 1252 O LYS A 154 33.075 109.656 173.498 1.00 37.93 1253 N VAL A 155 33.941 108.831 175.411 1.00 29.99 1254 CA VAL A 155 32.935 109.355 176.314 1.00 9.34 1255 CB VAL A 155 32.099 108.223 176.890 1.00 21.29 1256 CG1 VAL A 155 31.048 108.748 177.826 1.00 23.90 1257 CG2 VAL A 155 31.476 107.478 175.791 1.00 37.70 1258 C VAL A 155 33.687 109.997 177.457 1.00 27.74 1259 O VAL A 155 34.312 109.306 178.262 1.00 13.56 1260 N TRP A 156 33.627 111.314 177.557 1.00 38.73 1261 CA TRP A 156 34.351 111.977 178.633 1.00 69.64 1262 CB TRP A 156 33.966 111.410 179.999 1.00 28.52 1263 CG TRP A 156 32.519 111.540 180.386 1.00 64.30 1264 CD2 TRP A 156 31.672 112.685 180.244 1.00 16.66 1265 CE2 TRP A 156 30.417 112.342 180.786 1.00 65.75 1266 CE3 TRP A 156 31.847 113.967 179.715 1.00 72.95 1267 CD1 TRP A 156 31.759 110.583 180.991 1.00 80.53 1268 NE1 TRP A 156 30.500 111.052 181.237 1.00 20.03 1269 CZ2 TRP A 156 29.348 113.232 180.808 1.00 14.24 1270 CZ3 TRP A 156 30.775 114.850 179.744 1.00 11.55 1271 CH2 TRP A 156 29.551 114.477 180.284 1.00 40.65 1272 C TRP A 156 35.834 111.721 178.407 1.00 58.02 1273 O TRP A 156 36.565 111.406 179.334 1.00 32.03 1274 N GLN A 157 36.254 111.828 177.154 1.00 29.52 1275 CA GLN A 157 37.647 111.654 176.770 1.00 71.13 1276 CB GLN A 157 38.515 112.648 177.532 1.00 21.16 1277 CG GLN A 157 38.719 113.952 176.766 1.00 47.59 1278 CD GLN A 157 38.945 115.134 177.676 1.00 106.91 1279 OE1 GLN A 157 39.737 115.068 178.626 1.00 62.17 1280 NE2 GLN A 157 38.254 116.237 177.390 1.00 132.54 1281 C GLN A 157 38.273 110.271 176.820 1.00 20.80 1282 O GLN A 157 39.389 110.086 176.338 1.00 50.51 1283 N LEU A 158 37.569 109.299 177.380 1.00 41.89 1284 CA LEU A 158 38.096 107.940 177.410 1.00 24.44 1285 CB LEU A 158 37.826 107.303 178.761 1.00 29.61 1286 CG LEU A 158 38.450 108.159 179.850 1.00 5.42 1287 CD1 LEU A 158 38.603 107.360 181.127 1.00 45.69 1288 CD2 LEU A 158 39.806 108.640 179.378 1.00 68.22 1289 C LEU A 158 37.525 107.073 176.281 1.00 69.39 1290 O LEU A 158 36.521 107.420 175.653 1.00 33.83 1291 N ASP A 159 38.163 105.938 176.024 1.00 33.70 1292 CA ASP A 159 37.723 105.088 174.933 1.00 15.27 1293 CB ASP A 159 38.940 104.625 174.126 1.00 72.08 1294 CG ASP A 159 39.602 105.757 173.350 1.00 44.73 1295 OD1 ASP A 159 38.896 106.450 172.601 1.00 81.88 1296 OD2 ASP A 159 40.830 105.951 173.470 1.00 105.33 1297 C ASP A 159 36.897 103.886 175.355 1.00 50.78 1298 O ASP A 159 37.192 103.224 176.356 1.00 42.36 1299 N TYR A 160 35.859 103.602 174.577 1.00 14.41 1300 CA TYR A 160 35.006 102.466 174.875 1.00 19.18 1301 CB TYR A 160 33.779 102.923 175.654 1.00 30.10 1302 CG TYR A 160 34.112 103.527 177.002 1.00 39.60 1303 CD1 TYR A 160 34.388 104.884 177.140 1.00 9.47 1304 CE1 TYR A 160 34.750 105.418 178.371 1.00 50.45 1305 CD2 TYR A 160 34.198 102.725 178.131 1.00 36.31 1306 CE2 TYR A 160 34.551 103.247 179.361 1.00 31.00 1307 CZ TYR A 160 34.830 104.587 179.480 1.00 32.81 1308 OH TYR A 160 35.206 105.063 180.718 1.00 38.13 1309 C TYR A 160 34.583 101.703 173.629 1.00 62.53 1310 O TYR A 160 34.549 102.246 172.520 1.00 45.60 1311 N GLU A 161 34.249 100.435 173.824 1.00 46.69 1312 CA GLU A 161 33.852 99.563 172.727 1.00 47.10 1313 CB GLU A 161 35.018 98.620 172.417 1.00 44.91 1314 CG GLU A 161 34.882 97.745 171.191 1.00 102.74 1315 CD GLU A 161 36.108 96.855 170.973 1.00 98.25 1316 OE1 GLU A 161 36.103 96.032 170.030 1.00 115.20 1317 OE2 GLU A 161 37.079 96.980 171.749 1.00 83.84 1318 C GLU A 161 32.617 98.782 173.181 1.00 57.73 1319 O GLU A 161 32.586 98.245 174.284 1.00 75.56 1320 N SER A 162 31.594 98.741 172.337 1.00 36.86 1321 CA SER A 162 30.355 98.038 172.646 1.00 24.23 1322 CB SER A 162 29.258 98.474 171.679 1.00 85.17 1323 OG SER A 162 29.691 98.382 170.325 1.00 33.98 1324 C SER A 162 30.546 96.549 172.518 1.00 41.42 1325 O SER A 162 31.379 96.108 171.739 1.00 40.06 1326 N GLU A 163 29.828 95.793 173.363 1.00 47.31 1327 CA GLU A 163 29.945 94.371 173.069 1.00 32.63 1328 CB GLU A 163 29.169 93.547 174.097 1.00 99.44 1329 CG GLU A 163 29.649 93.729 175.527 1.00 204.45 1330 CD GLU A 163 28.850 92.906 176.519 1.00 213.27 1331 OE1 GLU A 163 27.925 92.187 176.086 1.00 189.41 1332 OE2 GLU A 163 29.148 92.980 177.729 1.00 180.03 1333 C GLU A 163 29.462 94.059 171.657 1.00 38.80 1334 O GLU A 163 28.601 94.902 171.253 1.00 51.57 1335 N PRO A 164 30.006 93.173 170.942 1.00 52.67 1336 CD PRO A 164 30.968 92.184 171.457 1.00 85.33 1337 CA PRO A 164 29.650 92.869 169.551 1.00 18.17 1338 CB PRO A 164 30.698 91.847 169.156 1.00 48.35 1339 CG PRO A 164 30.886 91.089 170.416 1.00 83.53 1340 C PRO A 164 28.238 92.378 169.300 1.00 33.91 1341 O PRO A 164 27.605 91.799 170.180 1.00 41.04 1342 N LEU A 165 27.760 92.592 168.077 1.00 50.63 1343 CA LEU A 165 26.402 92.200 167.706 1.00 22.85 1344 CB LEU A 165 25.483 93.404 167.777 1.00 65.50 1345 CG LEU A 165 24.027 93.057 167.530 1.00 5.42 1346 CD1 LEU A 165 23.591 92.064 168.578 1.00 85.48 1347 CD2 LEU A 165 23.182 94.310 167.584 1.00 73.11 1348 C LEU A 165 26.254 91.591 166.323 1.00 58.98 1349 O LEU A 165 26.696 92.171 165.326 1.00 45.85 1350 N ASN A 166 25.586 90.441 166.269 1.00 60.58 1351 CA ASN A 166 25.362 89.731 165.018 1.00 45.14 1352 CB ASN A 166 25.362 88.226 165.258 1.00 79.77 1353 CG ASN A 166 26.748 87.681 165.468 1.00 84.12 1354 OD1 ASN A 166 27.672 88.071 164.756 1.00 37.27 1355 ND2 ASN A 166 26.900 86.775 166.428 1.00 83.10 1356 C ASN A 166 24.079 90.124 164.312 1.00 53.27 1357 O ASN A 166 23.018 90.241 164.919 1.00 65.38 1358 N ILE A 167 24.195 90.314 163.008 1.00 52.39 1359 CA ILE A 167 23.071 90.689 162.171 1.00 51.60 1360 CB ILE A 167 23.197 92.152 161.735 1.00 54.96 1361 CG2 ILE A 167 22.259 92.454 160.598 1.00 34.47 1362 CG1 ILE A 167 22.875 93.055 162.912 1.00 29.93 1363 CD1 ILE A 167 23.061 94.512 162.595 1.00 110.11 1364 C ILE A 167 23.023 89.784 160.944 1.00 77.50 1365 O ILE A 167 24.024 89.605 160.245 1.00 94.63 1366 N THR A 168 21.844 89.226 160.691 1.00 79.37 1367 CA THR A 168 21.635 88.318 159.573 1.00 66.36 1368 CB THR A 168 21.250 86.945 160.109 1.00 55.12 1369 OG1 THR A 168 20.149 87.094 161.014 1.00 103.78 1370 CG2 THR A 168 22.416 86.313 160.856 1.00 86.09 1371 C THR A 168 20.545 88.797 158.607 1.00 74.59 1372 O THR A 168 19.565 89.412 159.024 1.00 64.58 1373 N VAL A 169 20.718 88.502 157.320 1.00 76.13 1374 CA VAL A 169 19.752 88.894 156.291 1.00 70.39 1375 CB VAL A 169 20.320 90.056 155.456 1.00 62.07 1376 CG1 VAL A 169 19.381 90.419 154.335 1.00 100.15 1377 CG2 VAL A 169 20.529 91.251 156.341 1.00 62.65 1378 C VAL A 169 19.382 87.703 155.386 1.00 94.90 1379 O VAL A 169 20.259 86.968 154.931 1.00 115.53 1380 N ILE A 170 18.081 87.537 155.123 1.00 88.61 1381 CA ILE A 170 17.538 86.422 154.329 1.00 131.29 1382 CB ILE A 170 16.224 85.933 154.969 1.00 132.04 1383 CG2 ILE A 170 15.908 84.511 154.513 1.00 178.52 1384 CG1 ILE A 170 16.360 85.966 156.492 1.00 77.40 1385 CD1 ILE A 170 15.077 85.661 157.225 1.00 74.21 1386 C ILE A 170 17.264 86.673 152.835 1.00 163.13 1387 O ILE A 170 17.487 87.768 152.330 1.00 191.77 1388 N LYS A 171 16.781 85.637 152.142 1.00 174.37 1389 CA LYS A 171 16.446 85.699 150.713 1.00 184.81 1390 CB LYS A 171 17.572 85.098 149.861 1.00 169.16 1391 CG LYS A 171 18.821 85.950 149.771 1.00 171.69 1392 CD LYS A 171 19.841 85.352 148.814 1.00 165.73 1393 CE LYS A 171 21.059 86.259 148.692 1.00 166.52 1394 NZ LYS A 171 22.110 85.721 147.784 1.00 163.94 1395 C LYS A 171 15.152 84.928 150.430 1.00 199.02 1396 O LYS A 171 14.841 83.961 151.124 1.00 217.89 1397 N ALA A 172 14.405 85.349 149.410 1.00 194.74 1398 CA ALA A 172 13.152 84.681 149.047 1.00 171.94 1399 CB ALA A 172 11.960 85.501 149.535 1.00 113.16 1400 C ALA A 172 13.055 84.474 147.535 1.00 174.40 1401 O ALA A 172 12.810 85.420 146.788 1.00 182.27 1402 N PRO A 173 13.241 83.227 147.067 1.00 195.13 1403 CD PRO A 173 13.548 82.010 147.842 1.00 150.42 1404 CA PRO A 173 13.170 82.925 145.632 1.00 196.30 1405 CB PRO A 173 13.702 81.495 145.558 1.00 174.85 1406 CG PRO A 173 13.235 80.907 146.852 1.00 159.72 1407 C PRO A 173 11.765 83.064 145.034 1.00 184.97 1408 O PRO A 173 11.238 82.054 144.522 1.00 174.19 1409 OXT PRO A 173 11.213 84.183 145.089 1.00 91.11 1410 C1 NAG A 221 11.009 106.713 181.607 1.00 78.57 1411 C2 NAG A 221 11.997 107.878 181.655 1.00 100.89 1412 N2 NAG A 221 13.311 107.471 181.201 1.00 76.21 1413 C7 NAG A 221 13.976 108.256 180.361 1.00 117.38 1414 O7 NAG A 221 13.803 108.231 179.142 1.00 148.10 1415 C8 NAG A 221 14.971 109.233 180.966 1.00 135.41 1416 C3 NAG A 221 12.062 108.405 183.087 1.00 127.09 1417 O3 NAG A 221 12.916 109.541 183.151 1.00 152.40 1418 C4 NAG A 221 10.653 108.784 183.562 1.00 126.14 1419 O4 NAG A 221 10.688 109.080 184.970 1.00 148.94 1420 C5 NAG A 221 9.653 107.645 183.321 1.00 133.04 1421 O5 NAG A 221 9.707 107.189 181.953 1.00 70.49 1422 C6 NAG A 221 8.220 108.040 183.621 1.00 149.52 1423 O6 NAG A 221 7.694 108.868 182.567 1.00 151.09 1424 C1 NAG A 222 10.235 110.337 185.310 1.00 150.76 1425 C2 NAG A 222 9.719 110.337 186.759 1.00 157.88 1426 N2 NAG A 222 8.580 109.445 186.884 1.00 152.33 1427 C7 NAG A 222 8.427 108.704 187.977 1.00 149.05 1428 O7 NAG A 222 9.078 107.677 188.190 1.00 108.16 1429 C8 NAG A 222 7.395 109.174 188.991 1.00 148.72 1430 C3 NAG A 222 9.316 111.762 187.139 1.00 163.52 1431 O3 NAG A 222 8.887 111.804 188.493 1.00 159.10 1432 C4 NAG A 222 10.521 112.683 186.929 1.00 168.36 1433 O4 NAG A 222 10.184 114.036 187.276 1.00 195.32 1434 C5 NAG A 222 10.970 112.600 185.466 1.00 142.19 1435 O5 NAG A 222 11.333 111.244 185.156 1.00 131.31 1436 C6 NAG A 222 12.167 113.462 185.127 1.00 147.99 1437 O6 NAG A 222 12.730 113.081 183.879 1.00 139.76 1438 C1 MAN A 223 10.805 114.503 188.420 1.00 185.67 1439 C2 MAN A 223 10.910 116.025 188.373 1.00 183.28 1440 O2 MAN A 223 9.623 116.596 188.179 1.00 182.05 1441 C3 MAN A 223 11.524 116.542 189.677 1.00 206.08 1442 O3 MAN A 223 11.463 117.961 189.691 1.00 200.83 1443 C4 MAN A 223 10.787 115.976 190.907 1.00 228.59 1444 O4 MAN A 223 11.500 116.305 192.093 1.00 213.28 1445 C5 MAN A 223 10.646 114.450 190.805 1.00 211.66 1446 O5 MAN A 223 10.026 114.090 189.551 1.00 206.15 1447 C6 MAN A 223 9.793 113.860 191.919 1.00 191.52 1448 O6 MAN A 223 8.598 113.277 191.412 1.00 161.92 1449 C1 FUC A 224 7.359 110.170 182.978 1.00 147.50 1450 C2 FUC A 224 6.361 110.756 181.982 1.00 163.07 1451 O2 FUC A 224 6.901 110.689 180.670 1.00 142.50 1452 C3 FUC A 224 5.059 109.950 182.059 1.00 147.28 1453 O3 FUC A 224 4.101 110.474 181.149 1.00 122.66 1454 C4 FUC A 224 4.509 109.992 183.492 1.00 181.93 1455 O4 FUC A 224 4.136 111.323 183.829 1.00 194.01 1456 C5 FUC A 224 5.573 109.491 184.480 1.00 172.04 1457 O5 FUC A 224 6.810 110.224 184.301 1.00 162.84 1458 C6 FUC A 224 5.158 109.661 185.932 1.00 120.33 1459 C1 NAG A 242 13.815 85.747 181.704 1.00 57.19 1460 C2 NAG A 242 13.676 86.167 183.149 1.00 45.95 1461 N2 NAG A 242 12.332 86.630 183.415 1.00 15.33 1462 C7 NAG A 242 11.817 86.468 184.631 1.00 112.91 1463 O7 NAG A 242 11.620 85.356 185.127 1.00 100.48 1464 C8 NAG A 242 11.482 87.721 185.427 1.00 16.99 1465 C3 NAG A 242 14.703 87.257 183.411 1.00 60.32 1466 O3 NAG A 242 14.623 87.699 184.764 1.00 42.86 1467 C4 NAG A 242 16.114 86.722 183.109 1.00 61.08 1468 O4 NAG A 242 17.042 87.825 183.150 1.00 83.57 1469 C5 NAG A 242 16.181 86.065 181.715 1.00 41.47 1470 O5 NAG A 242 15.096 85.134 181.520 1.00 54.87 1471 C6 NAG A 242 17.467 85.288 181.499 1.00 119.52 1472 O6 NAG A 242 17.381 83.969 182.022 1.00 140.01 1473 C1 NAG A 243 18.183 87.704 183.928 1.00 81.48 1474 C2 NAG A 243 19.362 88.235 183.120 1.00 38.25 1475 N2 NAG A 243 19.591 87.363 181.993 1.00 69.21 1476 C7 NAG A 243 19.577 87.863 180.768 1.00 66.57 1477 O7 NAG A 243 19.393 89.057 180.540 1.00 94.86 1478 C8 NAG A 243 19.805 86.892 179.623 1.00 48.41 1479 C3 NAG A 243 20.625 88.312 183.964 1.00 87.22 1480 O3 NAG A 243 21.674 88.894 183.208 1.00 98.62 1481 C4 NAG A 243 20.364 89.143 185.212 1.00 76.30 1482 O4 NAG A 243 21.549 89.126 186.040 1.00 94.39 1483 C5 NAG A 243 19.170 88.509 185.959 1.00 102.39 1484 O5 NAG A 243 17.998 88.494 185.115 1.00 49.63 1485 C6 NAG A 243 18.782 89.210 187.244 1.00 122.15 1486 O6 NAG A 243 17.997 88.358 188.067 1.00 105.32 1487 C1 MAN A 244 22.078 90.350 186.412 1.00 64.85 1488 C2 MAN A 244 22.728 90.214 187.783 1.00 116.22 1489 O2 MAN A 244 23.684 89.161 187.744 1.00 77.96 1490 C3 MAN A 244 23.402 91.540 188.186 1.00 112.21 1491 O3 MAN A 244 24.150 91.370 189.413 1.00 152.31 1492 C4 MAN A 244 24.351 92.024 187.075 1.00 144.57 1493 O4 MAN A 244 24.813 93.333 187.385 1.00 193.98 1494 C5 MAN A 244 23.633 92.031 185.713 1.00 57.60 1495 O5 MAN A 244 23.067 90.728 185.441 1.00 80.63 1496 C6 MAN A 244 24.504 92.436 184.513 1.00 53.28 1497 O6 MAN A 244 25.641 91.560 184.352 1.00 64.48 1498 C1 MAN A 245 23.427 91.459 190.614 1.00 134.73 1499 C2 MAN A 245 24.400 91.435 191.803 1.00 145.85 1500 O2 MAN A 245 23.715 91.778 193.000 1.00 115.81 1501 C3 MAN A 245 25.063 90.050 191.951 1.00 134.74 1502 O3 MAN A 245 25.754 89.986 193.192 1.00 105.27 1503 C4 MAN A 245 24.043 88.898 191.885 1.00 133.62 1504 O4 MAN A 245 24.736 87.669 191.714 1.00 67.76 1505 C5 MAN A 245 23.061 89.079 190.719 1.00 165.40 1506 O5 MAN A 245 22.479 90.403 190.751 1.00 164.09 1507 C6 MAN A 245 21.918 88.081 190.747 1.00 136.99 1508 O6 MAN A 245 20.800 88.600 191.453 1.00 163.94 1509 C1 MAN A 246 26.745 92.247 183.813 1.00 91.80 1510 C2 MAN A 246 27.492 91.359 182.813 1.00 89.53 1511 O2 MAN A 246 28.434 92.147 182.107 1.00 75.32 1512 C3 MAN A 246 28.223 90.227 183.536 1.00 97.98 1513 O3 MAN A 246 28.995 89.485 182.603 1.00 123.68 1514 C4 MAN A 246 29.139 90.790 184.628 1.00 99.73 1515 O4 MAN A 246 29.701 89.712 185.368 1.00 70.44 1516 C5 MAN A 246 28.338 91.709 185.566 1.00 111.67 1517 O5 MAN A 246 27.651 92.738 184.808 1.00 73.91 1518 C6 MAN A 246 29.187 92.408 186.620 1.00 133.93 1519 O6 MAN A 246 30.118 93.314 186.037 1.00 157.23 1520 C1 NAG A 366 28.056 85.901 166.422 1.00 118.02 1521 C2 NAG A 366 27.711 84.597 167.109 1.00 144.13 1522 N2 NAG A 366 27.168 84.844 168.429 1.00 145.90 1523 C7 NAG A 366 26.706 83.827 169.147 1.00 187.35 1524 O7 NAG A 366 27.404 83.211 169.952 1.00 194.87 1525 C8 NAG A 366 25.255 83.418 168.931 1.00 170.13 1526 C3 NAG A 366 28.966 83.736 167.196 1.00 142.04 1527 O3 NAG A 366 28.630 82.485 167.776 1.00 194.55 1528 C4 NAG A 366 29.556 83.514 165.790 1.00 143.64 1529 O4 NAG A 366 30.849 82.871 165.890 1.00 198.08 1530 C5 NAG A 366 29.712 84.852 165.035 1.00 84.06 1531 O5 NAG A 366 28.487 85.621 165.083 1.00 133.37 1532 C6 NAG A 366 30.057 84.664 163.560 1.00 113.91 1533 O6 NAG A 366 29.035 83.880 162.905 1.00 159.48 1534 C1 NAG A 367 30.856 81.509 166.161 1.00 189.45 1535 C2 NAG A 367 32.125 80.858 165.606 1.00 164.69 1536 N2 NAG A 367 32.162 81.012 164.163 1.00 194.38 1537 C7 NAG A 367 33.110 81.749 163.590 1.00 201.09 1538 O7 NAG A 367 33.517 82.807 164.072 1.00 175.40 1539 C8 NAG A 367 33.703 81.229 162.288 1.00 186.30 1540 C3 NAG A 367 32.134 79.368 165.981 1.00 171.43 1541 O3 NAG A 367 33.372 78.785 165.603 1.00 182.11 1542 C4 NAG A 367 31.925 79.180 167.489 1.00 181.87 1543 O4 NAG A 367 31.768 77.799 167.780 1.00 183.58 1544 C5 NAG A 367 30.683 79.946 167.949 1.00 186.74 1545 O5 NAG A 367 30.802 81.334 167.581 1.00 198.91 1546 C6 NAG A 367 30.463 79.898 169.448 1.00 186.99 1547 O6 NAG A 367 29.081 79.771 169.756 1.00 172.34 1548 C1 FUC A 369 29.475 83.367 161.677 1.00 178.37 1549 C2 FUC A 369 28.873 81.974 161.447 1.00 178.90 1550 O2 FUC A 369 29.095 81.158 162.587 1.00 137.53 1551 C3 FUC A 369 27.373 82.084 161.176 1.00 178.26 1552 O3 FUC A 369 26.837 80.797 160.906 1.00 126.18 1553 C4 FUC A 369 27.145 83.010 159.982 1.00 193.60 1554 O4 FUC A 369 27.752 82.452 158.825 1.00 190.82 1555 C5 FUC A 369 27.765 84.381 160.283 1.00 182.89 1556 O5 FUC A 369 29.175 84.233 160.576 1.00 193.18 1557 C6 FUC A 369 27.641 85.357 159.126 1.00 137.51 1558 CB PRO B 328 44.233 128.245 175.766 1.00 170.67 1559 CG PRO B 328 43.202 128.349 176.889 1.00 177.05 1560 C PRO B 328 43.060 126.964 173.946 1.00 208.41 1561 O PRO B 328 43.981 126.261 173.518 1.00 173.87 1562 N PRO B 328 42.116 129.063 174.936 1.00 199.93 1563 CD PRO B 328 42.170 129.366 176.377 1.00 189.57 1564 CA PRO B 328 43.348 128.347 174.529 1.00 198.40 1565 N CYS B 329 41.785 126.575 173.931 1.00 223.49 1566 CA CYS B 329 41.399 125.277 173.386 1.00 213.48 1567 C CYS B 329 40.595 125.390 172.094 1.00 210.28 1568 O CYS B 329 39.925 124.441 171.686 1.00 203.81 1569 CB CYS B 329 40.596 124.462 174.402 1.00 202.41 1570 SG CYS B 329 40.352 122.737 173.856 1.00 228.51 1571 N ASP B 330 40.647 126.557 171.461 1.00 211.89 1572 CA ASP B 330 39.960 126.766 170.189 1.00 192.96 1573 CB ASP B 330 39.714 128.266 169.964 1.00 206.60 1574 CG ASP B 330 38.919 128.560 168.691 1.00 207.78 1575 OD1 ASP B 330 39.428 128.310 167.577 1.00 198.18 1576 OD2 ASP B 330 37.778 129.052 168.806 1.00 197.14 1577 C ASP B 330 40.978 126.228 169.184 1.00 177.46 1578 O ASP B 330 41.198 126.802 168.117 1.00 190.87 1579 N SER B 331 41.601 125.110 169.550 1.00 151.57 1580 CA SER B 331 42.636 124.492 168.731 1.00 109.39 1581 CB SER B 331 43.959 124.493 169.509 1.00 109.57 1582 OG SER B 331 43.867 123.728 170.706 1.00 75.56 1583 C SER B 331 42.353 123.073 168.245 1.00 79.09 1584 O SER B 331 43.245 122.411 167.724 1.00 130.44 1585 N ASN B 332 41.129 122.596 168.411 1.00 76.72 1586 CA ASN B 332 40.796 121.246 167.977 1.00 39.06 1587 CB ASN B 332 40.842 120.285 169.162 1.00 93.86 1588 CG ASN B 332 42.247 119.821 169.484 1.00 76.70 1589 OD1 ASN B 332 43.185 120.617 169.523 1.00 81.95 1590 ND2 ASN B 332 42.398 118.525 169.735 1.00 60.32 1591 C ASN B 332 39.424 121.189 167.336 1.00 50.77 1592 O ASN B 332 38.588 120.357 167.696 1.00 48.39 1593 N PRO B 333 39.173 122.079 166.373 1.00 10.22 1594 CD PRO B 333 40.098 123.063 165.794 1.00 26.58 1595 CA PRO B 333 37.889 122.113 165.689 1.00 43.44 1596 CB PRO B 333 38.232 122.764 164.362 1.00 11.09 1597 CG PRO B 333 39.219 123.787 164.780 1.00 73.63 1598 C PRO B 333 37.271 120.738 165.530 1.00 11.84 1599 O PRO B 333 37.932 119.767 165.206 1.00 62.32 1600 N ARG B 334 35.984 120.677 165.788 1.00 33.64 1601 CA ARG B 334 35.235 119.460 165.677 1.00 33.31 1602 CB ARG B 334 34.754 119.322 164.242 1.00 10.21 1603 CG ARG B 334 33.904 118.112 164.022 1.00 52.28 1604 CD ARG B 334 32.439 118.403 163.975 1.00 10.85 1605 NE ARG B 334 31.983 118.450 162.597 1.00 39.50 1606 CZ ARG B 334 30.763 118.103 162.210 1.00 75.73 1607 NH1 ARG B 334 29.885 117.676 163.099 1.00 59.45 1608 NH2 ARG B 334 30.416 118.202 160.936 1.00 61.90 1609 C ARG B 334 36.002 118.225 166.156 1.00 35.54 1610 O ARG B 334 35.615 117.090 165.891 1.00 57.63 1611 N GLY B 335 37.081 118.441 166.896 1.00 21.32 1612 CA GLY B 335 37.832 117.308 167.413 1.00 60.66 1613 C GLY B 335 39.060 116.972 166.600 1.00 46.23 1614 O GLY B 335 39.953 116.256 167.053 1.00 28.43 1615 N VAL B 336 39.087 117.491 165.381 1.00 51.37 1616 CA VAL B 336 40.196 117.306 164.454 1.00 36.83 1617 CB VAL B 336 39.836 117.952 163.124 1.00 62.63 1618 CG1 VAL B 336 41.025 117.972 162.204 1.00 75.33 1619 CG2 VAL B 336 38.674 117.213 162.512 1.00 96.26 1620 C VAL B 336 41.485 117.947 164.969 1.00 35.62 1621 O VAL B 336 41.596 119.164 164.967 1.00 59.08 1622 N SER B 337 42.456 117.148 165.404 1.00 44.91 1623 CA SER B 337 43.714 117.712 165.900 1.00 35.01 1624 CB SER B 337 44.232 116.895 167.081 1.00 70.32 1625 OG SER B 337 44.222 115.512 166.795 1.00 72.41 1626 C SER B 337 44.791 117.806 164.809 1.00 48.70 1627 O SER B 337 44.673 117.177 163.760 1.00 25.48 1628 N ALA B 338 45.827 118.612 165.058 1.00 48.51 1629 CA ALA B 338 46.939 118.821 164.107 1.00 82.57 1630 CB ALA B 338 46.705 120.063 163.245 1.00 7.76 1631 C ALA B 338 48.260 118.980 164.842 1.00 29.51 1632 O ALA B 338 48.301 119.477 165.968 1.00 84.58 1633 N TYR B 339 49.340 118.555 164.206 1.00 63.43 1634 CA TYR B 339 50.643 118.655 164.823 1.00 60.91 1635 CB TYR B 339 51.122 117.269 165.235 1.00 46.03 1636 CG TYR B 339 50.150 116.534 166.132 1.00 43.69 1637 CD1 TYR B 339 49.014 115.921 165.614 1.00 74.02 1638 CE1 TYR B 339 48.098 115.288 166.440 1.00 48.18 1639 CD2 TYR B 339 50.347 116.492 167.503 1.00 70.23 1640 CE2 TYR B 339 49.435 115.867 168.340 1.00 97.07 1641 CZ TYR B 339 48.310 115.270 167.804 1.00 86.05 1642 OH TYR B 339 47.383 114.696 168.648 1.00 102.25 1643 C TYR B 339 51.610 119.290 163.841 1.00 88.66 1644 O TYR B 339 51.530 119.048 162.640 1.00 48.34 1645 N LEU B 340 52.515 120.118 164.348 1.00 69.25 1646 CA LEU B 340 53.476 120.776 163.479 1.00 62.80 1647 CB LEU B 340 53.186 122.263 163.438 1.00 27.87 1648 CG LEU B 340 54.027 123.160 162.544 1.00 34.78 1649 CD1 LEU B 340 53.820 122.802 161.089 1.00 68.67 1650 CD2 LEU B 340 53.615 124.594 162.770 1.00 83.17 1651 C LEU B 340 54.881 120.531 163.988 1.00 79.88 1652 O LEU B 340 55.294 121.133 164.972 1.00 77.02 1653 N SER B 341 55.612 119.651 163.305 1.00 82.92 1654 CA SER B 341 56.964 119.290 163.712 1.00 91.09 1655 CB SER B 341 57.333 117.925 163.139 1.00 105.90 1656 OG SER B 341 58.517 117.431 163.744 1.00 156.83 1657 C SER B 341 58.023 120.306 163.321 1.00 86.74 1658 O SER B 341 57.918 120.956 162.286 1.00 74.60 1659 N ARG B 342 59.045 120.419 164.168 1.00 108.27 1660 CA ARG B 342 60.165 121.343 163.976 1.00 58.14 1661 CB ARG B 342 60.602 121.890 165.343 1.00 98.53 1662 CG ARG B 342 60.649 120.808 166.429 1.00 141.70 1663 CD ARG B 342 61.354 121.239 167.726 1.00 145.30 1664 NE ARG B 342 60.568 122.139 168.567 1.00 104.32 1665 CZ ARG B 342 60.430 123.442 168.351 1.00 124.08 1666 NH1 ARG B 342 61.028 124.015 167.315 1.00 83.45 1667 NH2 ARG B 342 59.691 124.174 169.173 1.00 139.46 1668 C ARG B 342 61.352 120.635 163.287 1.00 98.70 1669 O ARG B 342 61.582 119.441 163.500 1.00 94.69 1670 N PRO B 343 62.120 121.368 162.457 1.00 62.71 1671 CD PRO B 343 62.016 122.823 162.278 1.00 69.22 1672 CA PRO B 343 63.281 120.850 161.728 1.00 36.63 1673 CB PRO B 343 63.916 122.104 161.148 1.00 63.75 1674 CG PRO B 343 62.776 123.035 161.003 1.00 46.63 1675 C PRO B 343 64.234 120.174 162.689 1.00 50.31 1676 O PRO B 343 64.518 120.713 163.762 1.00 73.12 1677 N SER B 344 64.737 119.002 162.311 1.00 83.43 1678 CA SER B 344 65.671 118.289 163.177 1.00 70.61 1679 CB SER B 344 65.778 116.812 162.781 1.00 82.96 1680 OG SER B 344 66.324 116.661 161.483 1.00 84.14 1681 C SER B 344 67.024 118.946 163.041 1.00 65.68 1682 O SER B 344 67.334 119.517 161.998 1.00 50.07 1683 N PRO B 345 67.844 118.894 164.104 1.00 74.48 1684 CD PRO B 345 67.611 118.184 165.375 1.00 88.87 1685 CA PRO B 345 69.183 119.494 164.081 1.00 69.58 1686 CB PRO B 345 69.862 118.867 165.296 1.00 81.66 1687 CG PRO B 345 68.745 118.694 166.255 1.00 59.69 1688 C PRO B 345 69.849 119.065 162.789 1.00 83.15 1689 O PRO B 345 70.233 119.893 161.960 1.00 54.26 1690 N PHE B 346 69.955 117.745 162.642 1.00 65.25 1691 CA PHE B 346 70.542 117.099 161.482 1.00 38.65 1692 CB PHE B 346 70.209 115.611 161.522 1.00 67.61 1693 CG PHE B 346 70.755 114.839 160.365 1.00 96.31 1694 CD1 PHE B 346 72.119 114.727 160.181 1.00 76.06 1695 CD2 PHE B 346 69.903 114.239 159.445 1.00 132.61 1696 CE1 PHE B 346 72.632 114.039 159.104 1.00 96.72 1697 CE2 PHE B 346 70.410 113.544 158.358 1.00 124.94 1698 CZ PHE B 346 71.779 113.445 158.187 1.00 134.65 1699 C PHE B 346 70.045 117.721 160.170 1.00 58.29 1700 O PHE B 346 70.796 118.379 159.474 1.00 57.14 1701 N ASP B 347 68.777 117.524 159.831 1.00 56.88 1702 CA ASP B 347 68.226 118.078 158.592 1.00 64.19 1703 CB ASP B 347 66.703 117.859 158.542 1.00 98.15 1704 CG ASP B 347 66.318 116.431 158.211 1.00 120.11 1705 OD1 ASP B 347 66.506 116.024 157.046 1.00 142.93 1706 OD2 ASP B 347 65.826 115.715 159.112 1.00 148.42 1707 C ASP B 347 68.509 119.576 158.466 1.00 78.62 1708 O ASP B 347 68.339 120.174 157.401 1.00 40.12 1709 N LEU B 348 68.969 120.178 159.550 1.00 43.72 1710 CA LEU B 348 69.184 121.613 159.553 1.00 79.44 1711 CB LEU B 348 68.570 122.183 160.837 1.00 64.43 1712 CG LEU B 348 68.601 123.691 161.101 1.00 74.91 1713 CD1 LEU B 348 68.208 124.482 159.860 1.00 80.89 1714 CD2 LEU B 348 67.656 123.985 162.246 1.00 82.45 1715 C LEU B 348 70.617 122.094 159.396 1.00 77.53 1716 O LEU B 348 70.863 123.165 158.841 1.00 66.37 1717 N PHE B 349 71.560 121.300 159.877 1.00 81.75 1718 CA PHE B 349 72.964 121.666 159.811 1.00 90.94 1719 CB PHE B 349 73.515 121.657 161.221 1.00 89.74 1720 CG PHE B 349 72.864 122.665 162.096 1.00 88.86 1721 CD1 PHE B 349 72.745 122.458 163.464 1.00 102.92 1722 CD2 PHE B 349 72.363 123.837 161.542 1.00 48.94 1723 CE1 PHE B 349 72.133 123.406 164.274 1.00 64.93 1724 CE2 PHE B 349 71.754 124.786 162.335 1.00 94.98 1725 CZ PHE B 349 71.638 124.572 163.708 1.00 102.89 1726 C PHE B 349 73.806 120.800 158.889 1.00 102.94 1727 O PHE B 349 74.633 121.304 158.137 1.00 120.26 1728 N ILE B 350 73.609 119.494 158.963 1.00 100.45 1729 CA ILE B 350 74.328 118.586 158.098 1.00 57.80 1730 CB ILE B 350 74.145 117.136 158.545 1.00 71.44 1731 CG2 ILE B 350 74.830 116.213 157.588 1.00 91.54 1732 CG1 ILE B 350 74.662 116.959 159.972 1.00 71.63 1733 CD1 ILE B 350 76.040 117.471 160.193 1.00 65.43 1734 C ILE B 350 73.672 118.752 156.738 1.00 76.53 1735 O ILE B 350 74.101 119.559 155.928 1.00 93.37 1736 N ARG B 351 72.601 117.998 156.520 1.00 76.58 1737 CA ARG B 351 71.852 118.003 155.261 1.00 85.35 1738 CB ARG B 351 70.544 117.223 155.464 1.00 94.17 1739 CG ARG B 351 69.978 116.539 154.229 1.00 114.26 1740 CD ARG B 351 69.081 115.375 154.644 1.00 134.12 1741 NE ARG B 351 68.530 114.661 153.497 1.00 180.07 1742 CZ ARG B 351 67.646 115.179 152.650 1.00 196.67 1743 NH1 ARG B 351 67.210 116.420 152.821 1.00 201.25 1744 NH2 ARG B 351 67.198 114.456 151.632 1.00 193.34 1745 C ARG B 351 71.563 119.406 154.722 1.00 85.97 1746 O ARG B 351 71.257 119.576 153.546 1.00 79.18 1747 N LYS B 352 71.672 120.401 155.594 1.00 70.30 1748 CA LYS B 352 71.417 121.800 155.249 1.00 116.58 1749 CB LYS B 352 72.641 122.404 154.559 1.00 144.96 1750 CG LYS B 352 73.881 122.501 155.448 1.00 168.84 1751 CD LYS B 352 74.894 123.491 154.874 1.00 186.41 1752 CE LYS B 352 76.217 123.484 155.633 1.00 172.60 1753 NZ LYS B 352 77.028 122.264 155.354 1.00 186.13 1754 C LYS B 352 70.162 122.102 154.416 1.00 119.94 1755 O LYS B 352 70.110 123.108 153.709 1.00 105.59 1756 N SER B 353 69.160 121.231 154.504 1.00 128.80 1757 CA SER B 353 67.884 121.411 153.802 1.00 102.46 1758 CB SER B 353 67.788 120.501 152.574 1.00 122.75 1759 OG SER B 353 67.784 119.131 152.936 1.00 168.70 1760 C SER B 353 66.811 121.034 154.818 1.00 99.64 1761 O SER B 353 66.337 119.897 154.860 1.00 93.09 1762 N PRO B 354 66.421 121.994 155.661 1.00 84.24 1763 CD PRO B 354 66.948 123.357 155.738 1.00 97.02 1764 CA PRO B 354 65.415 121.793 156.698 1.00 77.36 1765 CB PRO B 354 65.720 122.910 157.702 1.00 87.64 1766 CG PRO B 354 67.006 123.540 157.208 1.00 75.30 1767 C PRO B 354 63.998 121.894 156.181 1.00 95.66 1768 O PRO B 354 63.722 122.632 155.225 1.00 61.77 1769 N THR B 355 63.108 121.145 156.826 1.00 83.51 1770 CA THR B 355 61.696 121.153 156.478 1.00 60.49 1771 CB THR B 355 61.340 120.121 155.405 1.00 59.24 1772 OG1 THR B 355 61.685 118.810 155.876 1.00 77.07 1773 CG2 THR B 355 62.053 120.440 154.098 1.00 114.79 1774 C THR B 355 60.837 120.838 157.683 1.00 79.73 1775 O THR B 355 61.132 119.924 158.464 1.00 73.10 1776 N ILE B 356 59.765 121.613 157.815 1.00 73.22 1777 CA ILE B 356 58.801 121.449 158.891 1.00 76.70 1778 CB ILE B 356 58.351 122.805 159.441 1.00 47.99 1779 CG2 ILE B 356 59.496 123.453 160.194 1.00 83.94 1780 CG1 ILE B 356 57.861 123.691 158.294 1.00 66.86 1781 CD1 ILE B 356 57.478 125.075 158.729 1.00 80.08 1782 C ILE B 356 57.595 120.723 158.311 1.00 74.21 1783 O ILE B 356 57.290 120.849 157.110 1.00 45.14 1784 N THR B 357 56.898 119.978 159.164 1.00 59.52 1785 CA THR B 357 55.752 119.215 158.706 1.00 66.63 1786 CB THR B 357 56.095 117.748 158.697 1.00 60.44 1787 OG1 THR B 357 57.388 117.574 158.106 1.00 96.24 1788 CG2 THR B 357 55.066 116.981 157.904 1.00 78.11 1789 C THR B 357 54.494 119.395 159.534 1.00 65.25 1790 O THR B 357 54.525 119.290 160.762 1.00 62.91 1791 N CYS B 358 53.387 119.639 158.836 1.00 60.07 1792 CA CYS B 358 52.076 119.835 159.453 1.00 60.41 1793 C CYS B 358 51.260 118.568 159.245 1.00 47.28 1794 O CYS B 358 50.999 118.164 158.117 1.00 61.76 1795 CB CYS B 358 51.372 121.006 158.789 1.00 66.79 1796 SG CYS B 358 49.884 121.601 159.632 1.00 87.73 1797 N LEU B 359 50.862 117.934 160.334 1.00 55.07 1798 CA LEU B 359 50.102 116.700 160.248 1.00 25.58 1799 CB LEU B 359 50.884 115.602 160.956 1.00 60.22 1800 CG LEU B 359 50.116 114.353 161.371 1.00 17.72 1801 CD1 LEU B 359 49.435 113.786 160.175 1.00 49.40 1802 CD2 LEU B 359 51.037 113.345 162.002 1.00 86.18 1803 C LEU B 359 48.703 116.836 160.859 1.00 39.46 1804 O LEU B 359 48.538 117.114 162.044 1.00 57.72 1805 N VAL B 360 47.692 116.631 160.034 1.00 50.02 1806 CA VAL B 360 46.316 116.727 160.476 1.00 35.99 1807 CB VAL B 360 45.467 117.468 159.452 1.00 46.54 1808 CG1 VAL B 360 44.028 117.436 159.862 1.00 47.57 1809 CG2 VAL B 360 45.948 118.886 159.328 1.00 29.82 1810 C VAL B 360 45.751 115.334 160.628 1.00 34.08 1811 O VAL B 360 45.885 114.501 159.733 1.00 60.52 1812 N VAL B 361 45.102 115.091 161.759 1.00 22.24 1813 CA VAL B 361 44.520 113.790 162.040 1.00 37.22 1814 CB VAL B 361 45.305 113.117 163.163 1.00 11.28 1815 CG1 VAL B 361 46.626 113.793 163.312 1.00 37.36 1816 CG2 VAL B 361 44.563 113.194 164.430 1.00 36.29 1817 C VAL B 361 43.032 113.828 162.424 1.00 32.87 1818 O VAL B 361 42.504 114.859 162.814 1.00 47.67 1819 N ASP B 362 42.374 112.680 162.324 1.00 50.85 1820 CA ASP B 362 40.963 112.540 162.657 1.00 28.87 1821 CB ASP B 362 40.697 112.967 164.092 1.00 43.13 1822 CG ASP B 362 41.283 111.999 165.107 1.00 96.71 1823 OD1 ASP B 362 41.186 110.772 164.910 1.00 61.11 1824 OD2 ASP B 362 41.832 112.464 166.122 1.00 95.29 1825 C ASP B 362 39.978 113.227 161.726 1.00 39.54 1826 O ASP B 362 38.838 113.482 162.112 1.00 44.37 1827 N LEU B 363 40.410 113.513 160.500 1.00 30.82 1828 CA LEU B 363 39.536 114.118 159.506 1.00 21.83 1829 CB LEU B 363 40.328 114.589 158.298 1.00 31.47 1830 CG LEU B 363 41.130 115.877 158.418 1.00 45.22 1831 CD1 LEU B 363 42.030 116.037 157.201 1.00 61.55 1832 CD2 LEU B 363 40.174 117.029 158.514 1.00 33.26 1833 C LEU B 363 38.608 113.026 159.049 1.00 44.60 1834 O LEU B 363 38.922 111.859 159.163 1.00 46.41 1835 N ALA B 364 37.455 113.392 158.533 1.00 51.90 1836 CA ALA B 364 36.541 112.383 158.045 1.00 22.74 1837 CB ALA B 364 35.186 112.587 158.647 1.00 51.33 1838 C ALA B 364 36.464 112.500 156.530 1.00 60.62 1839 O ALA B 364 36.529 113.603 155.972 1.00 44.38 1840 N PRO B 365 36.339 111.365 155.837 1.00 18.39 1841 CD PRO B 365 35.980 110.033 156.333 1.00 51.04 1842 CA PRO B 365 36.255 111.404 154.379 1.00 40.07 1843 CB PRO B 365 35.930 109.963 154.027 1.00 109.08 1844 CG PRO B 365 35.117 109.531 155.214 1.00 40.87 1845 C PRO B 365 35.132 112.340 153.965 1.00 58.17 1846 O PRO B 365 34.127 112.428 154.672 1.00 50.80 1847 N SER B 366 35.303 113.028 152.833 1.00 35.27 1848 CA SER B 366 34.292 113.944 152.315 1.00 93.15 1849 CB SER B 366 34.314 115.271 153.076 1.00 108.06 1850 OG SER B 366 35.515 115.977 152.855 1.00 71.65 1851 C SER B 366 34.515 114.210 150.839 1.00 44.93 1852 O SER B 366 35.556 113.866 150.290 1.00 106.10 1853 N LYS B 367 33.529 114.827 150.198 1.00 130.17 1854 CA LYS B 367 33.600 115.155 148.779 1.00 79.40 1855 CB LYS B 367 32.319 115.878 148.331 1.00 125.03 1856 CG LYS B 367 31.050 115.020 148.296 1.00 164.89 1857 CD LYS B 367 29.862 115.815 147.732 1.00 160.83 1858 CE LYS B 367 28.612 114.952 147.548 1.00 137.20 1859 NZ LYS B 367 27.489 115.720 146.924 1.00 126.69 1860 C LYS B 367 34.806 116.040 148.477 1.00 52.10 1861 O LYS B 367 35.562 115.774 147.544 1.00 108.75 1862 N GLY B 368 34.986 117.089 149.272 1.00 66.48 1863 CA GLY B 368 36.093 117.999 149.043 1.00 81.03 1864 C GLY B 368 37.267 117.768 149.965 1.00 56.47 1865 O GLY B 368 37.106 117.247 151.062 1.00 92.39 1866 N THR B 369 38.455 118.154 149.516 1.00 59.57 1867 CA THR B 369 39.659 117.986 150.313 1.00 61.18 1868 CB THR B 369 40.891 117.867 149.416 1.00 71.21 1869 OG1 THR B 369 41.072 119.088 148.693 1.00 96.74 1870 CG2 THR B 369 40.710 116.731 148.420 1.00 106.84 1871 C THR B 369 39.802 119.215 151.181 1.00 47.36 1872 O THR B 369 39.091 120.193 150.985 1.00 60.95 1873 N VAL B 370 40.712 119.183 152.142 1.00 34.09 1874 CA VAL B 370 40.888 120.349 152.999 1.00 48.60 1875 CB VAL B 370 41.744 120.043 154.219 1.00 24.99 1876 CG1 VAL B 370 41.249 118.771 154.883 1.00 36.87 1877 CG2 VAL B 370 43.201 119.920 153.814 1.00 68.00 1878 C VAL B 370 41.552 121.468 152.225 1.00 25.41 1879 O VAL B 370 41.788 121.345 151.027 1.00 88.63 1880 N ASN B 371 41.866 122.554 152.915 1.00 53.72 1881 CA ASN B 371 42.477 123.715 152.290 1.00 52.65 1882 CB ASN B 371 41.401 124.794 152.091 1.00 74.57 1883 CG ASN B 371 41.906 126.001 151.353 1.00 115.17 1884 OD1 ASN B 371 43.097 126.127 151.082 1.00 164.46 1885 ND2 ASN B 371 40.996 126.917 151.034 1.00 174.36 1886 C ASN B 371 43.581 124.172 153.235 1.00 58.62 1887 O ASN B 371 43.409 125.079 154.042 1.00 79.32 1888 N LEU B 372 44.713 123.489 153.130 1.00 85.89 1889 CA LEU B 372 45.903 123.722 153.936 1.00 45.57 1890 CB LEU B 372 46.816 122.511 153.816 1.00 37.74 1891 CG LEU B 372 47.914 122.228 154.841 1.00 36.14 1892 CD1 LEU B 372 48.335 123.493 155.586 1.00 42.25 1893 CD2 LEU B 372 47.373 121.176 155.809 1.00 26.23 1894 C LEU B 372 46.605 124.937 153.369 1.00 69.02 1895 O LEU B 372 46.702 125.071 152.155 1.00 96.74 1896 N THR B 373 47.102 125.818 154.228 1.00 57.25 1897 CA THR B 373 47.760 127.025 153.748 1.00 31.14 1898 CB THR B 373 46.741 128.177 153.665 1.00 67.35 1899 OG1 THR B 373 45.708 127.832 152.735 1.00 72.32 1900 CG2 THR B 373 47.397 129.452 153.211 1.00 83.78 1901 C THR B 373 48.927 127.440 154.633 1.00 76.56 1902 O THR B 373 48.768 127.635 155.846 1.00 63.76 1903 N TRP B 374 50.099 127.578 154.010 1.00 81.63 1904 CA TRP B 374 51.325 127.962 154.715 1.00 63.39 1905 CB TRP B 374 52.533 127.246 154.128 1.00 60.06 1906 CG TRP B 374 52.577 125.801 154.393 1.00 38.27 1907 CD2 TRP B 374 53.047 125.173 155.583 1.00 17.81 1908 CE2 TRP B 374 52.925 123.781 155.398 1.00 26.57 1909 CE3 TRP B 374 53.563 125.650 156.784 1.00 45.86 1910 CD1 TRP B 374 52.195 124.796 153.549 1.00 58.25 1911 NE1 TRP B 374 52.403 123.575 154.149 1.00 41.78 1912 CZ2 TRP B 374 53.300 122.866 156.373 1.00 46.60 1913 CZ3 TRP B 374 53.940 124.734 157.759 1.00 44.09 1914 CH2 TRP B 374 53.804 123.364 157.548 1.00 18.32 1915 C TRP B 374 51.591 129.457 154.649 1.00 94.67 1916 O TRP B 374 51.341 130.096 153.622 1.00 70.49 1917 N SER B 375 52.133 130.003 155.735 1.00 79.04 1918 CA SER B 375 52.421 131.428 155.798 1.00 76.64 1919 CB SER B 375 51.136 132.190 156.128 1.00 121.29 1920 OG SER B 375 50.563 131.725 157.343 1.00 115.00 1921 C SER B 375 53.500 131.793 156.818 1.00 100.83 1922 O SER B 375 53.681 131.114 157.844 1.00 45.77 1923 N ARG B 376 54.215 132.876 156.526 1.00 84.64 1924 CA ARG B 376 55.263 133.366 157.418 1.00 89.30 1925 CB ARG B 376 56.525 133.715 156.631 1.00 108.51 1926 CG ARG B 376 57.394 132.526 156.294 1.00 125.68 1927 CD ARG B 376 58.852 132.940 156.133 1.00 127.76 1928 NE ARG B 376 59.165 133.476 154.812 1.00 88.17 1929 CZ ARG B 376 60.372 133.898 154.461 1.00 124.32 1930 NH1 ARG B 376 61.368 133.849 155.337 1.00 105.92 1931 NH2 ARG B 376 60.588 134.349 153.234 1.00 164.32 1932 C ARG B 376 54.795 134.607 158.167 1.00 120.27 1933 O ARG B 376 53.953 135.367 157.674 1.00 114.07 1934 N ALA B 377 55.344 134.817 159.357 1.00 101.03 1935 CA ALA B 377 54.973 135.981 160.151 1.00 108.48 1936 CB ALA B 377 55.394 135.784 161.583 1.00 88.56 1937 C ALA B 377 55.607 137.252 159.593 1.00 112.40 1938 O ALA B 377 55.071 138.345 159.751 1.00 124.37 1939 N SER B 378 56.753 137.105 158.943 1.00 101.18 1940 CA SER B 378 57.445 138.242 158.362 1.00 69.51 1941 CB SER B 378 58.845 137.831 157.902 1.00 111.91 1942 OG SER B 378 58.778 137.003 156.747 1.00 103.91 1943 C SER B 378 56.665 138.786 157.166 1.00 87.46 1944 O SER B 378 56.842 139.936 156.769 1.00 118.01 1945 N GLY B 379 55.807 137.957 156.588 1.00 90.70 1946 CA GLY B 379 55.031 138.392 155.441 1.00 104.68 1947 C GLY B 379 55.679 137.954 154.143 1.00 122.51 1948 O GLY B 379 55.045 137.946 153.084 1.00 110.08 1949 N LYS B 380 56.950 137.579 154.229 1.00 122.20 1950 CA LYS B 380 57.699 137.136 153.061 1.00 147.83 1951 CB LYS B 380 59.174 136.966 153.428 1.00 162.29 1952 CG LYS B 380 59.830 138.223 153.989 1.00 173.82 1953 CD LYS B 380 61.286 137.969 154.360 1.00 180.37 1954 CE LYS B 380 61.949 139.218 154.922 1.00 172.23 1955 NZ LYS B 380 63.378 138.976 155.269 1.00 155.65 1956 C LYS B 380 57.145 135.820 152.513 1.00 146.60 1957 O LYS B 380 56.856 134.897 153.270 1.00 157.16 1958 N PRO B 381 56.992 135.724 151.182 1.00 140.30 1959 CD PRO B 381 57.285 136.796 150.216 1.00 154.76 1960 CA PRO B 381 56.475 134.537 150.493 1.00 131.70 1961 CB PRO B 381 56.787 134.838 149.034 1.00 142.42 1962 CG PRO B 381 56.572 136.313 148.971 1.00 139.64 1963 C PRO B 381 57.085 133.216 150.966 1.00 119.70 1964 O PRO B 381 58.115 133.207 151.647 1.00 96.93 1965 N VAL B 382 56.443 132.109 150.589 1.00 110.70 1966 CA VAL B 382 56.885 130.765 150.975 1.00 88.04 1967 CB VAL B 382 55.908 130.140 151.964 1.00 67.75 1968 CG1 VAL B 382 55.938 130.895 153.273 1.00 128.08 1969 CG2 VAL B 382 54.511 130.160 151.360 1.00 82.52 1970 C VAL B 382 57.020 129.784 149.808 1.00 109.58 1971 O VAL B 382 56.279 129.858 148.817 1.00 109.44 1972 N ASN B 383 57.958 128.849 149.947 1.00 109.75 1973 CA ASN B 383 58.197 127.845 148.918 1.00 128.69 1974 CB ASN B 383 59.393 126.966 149.309 1.00 135.40 1975 CG ASN B 383 60.723 127.696 149.189 1.00 146.65 1976 OD1 ASN B 383 61.759 127.196 149.629 1.00 133.04 1977 ND2 ASN B 383 60.702 128.877 148.582 1.00 137.22 1978 C ASN B 383 56.955 126.981 148.730 1.00 91.22 1979 O ASN B 383 56.024 127.038 149.524 1.00 98.35 1980 N HIS B 384 56.937 126.189 147.668 1.00 93.62 1981 CA HIS B 384 55.806 125.312 147.411 1.00 67.76 1982 CB HIS B 384 55.861 124.821 145.971 1.00 86.21 1983 CG HIS B 384 55.759 125.923 144.968 1.00 106.64 1984 CD2 HIS B 384 56.710 126.691 144.388 1.00 118.02 1985 ND1 HIS B 384 54.551 126.390 144.500 1.00 70.58 1986 CE1 HIS B 384 54.760 127.398 143.676 1.00 107.89 1987 NE2 HIS B 384 56.063 127.602 143.590 1.00 141.17 1988 C HIS B 384 55.859 124.145 148.392 1.00 78.76 1989 O HIS B 384 56.936 123.688 148.786 1.00 62.48 1990 N SER B 385 54.694 123.665 148.801 1.00 90.92 1991 CA SER B 385 54.650 122.571 149.760 1.00 50.91 1992 CB SER B 385 53.664 122.908 150.880 1.00 71.25 1993 OG SER B 385 52.375 123.192 150.354 1.00 104.23 1994 C SER B 385 54.271 121.242 149.136 1.00 72.39 1995 O SER B 385 53.913 121.162 147.955 1.00 65.67 1996 N THR B 386 54.359 120.210 149.970 1.00 62.20 1997 CA THR B 386 54.036 118.826 149.632 1.00 53.65 1998 CB THR B 386 55.117 117.911 150.210 1.00 90.34 1999 OG1 THR B 386 56.193 117.804 149.269 1.00 80.69 2000 CG2 THR B 386 54.552 116.533 150.571 1.00 100.14 2001 C THR B 386 52.684 118.468 150.266 1.00 68.47 2002 O THR B 386 52.200 119.188 151.139 1.00 105.23 2003 N ARG B 387 52.063 117.377 149.837 1.00 56.81 2004 CA ARG B 387 50.795 117.008 150.437 1.00 54.80 2005 CB ARG B 387 49.720 118.013 150.006 1.00 49.15 2006 CG ARG B 387 48.321 117.671 150.466 1.00 66.87 2007 CD ARG B 387 47.403 118.853 150.339 1.00 67.37 2008 NE ARG B 387 46.030 118.490 150.645 1.00 77.86 2009 CZ ARG B 387 45.055 119.376 150.780 1.00 111.21 2010 NH1 ARG B 387 45.318 120.669 150.633 1.00 100.94 2011 NH2 ARG B 387 43.825 118.971 151.064 1.00 96.41 2012 C ARG B 387 50.347 115.582 150.128 1.00 56.65 2013 O ARG B 387 50.294 115.184 148.963 1.00 61.16 2014 N LYS B 388 50.035 114.816 151.177 1.00 36.92 2015 CA LYS B 388 49.555 113.441 151.016 1.00 59.67 2016 CB LYS B 388 50.560 112.426 151.556 1.00 30.37 2017 CG LYS B 388 52.019 112.796 151.452 1.00 148.33 2018 CD LYS B 388 52.864 111.704 152.106 1.00 145.55 2019 CE LYS B 388 54.353 112.005 152.019 1.00 171.95 2020 NZ LYS B 388 55.174 110.852 152.491 1.00 153.54 2021 C LYS B 388 48.290 113.253 151.835 1.00 56.48 2022 O LYS B 388 48.189 113.793 152.938 1.00 73.87 2023 N GLU B 389 47.339 112.480 151.324 1.00 33.78 2024 CA GLU B 389 46.120 112.216 152.086 1.00 52.94 2025 CB GLU B 389 44.889 112.865 151.423 1.00 32.75 2026 CG GLU B 389 44.856 114.388 151.542 1.00 138.12 2027 CD GLU B 389 43.709 115.017 150.776 1.00 167.38 2028 OE1 GLU B 389 42.548 114.596 150.983 1.00 151.81 2029 OE2 GLU B 389 43.977 115.938 149.971 1.00 152.33 2030 C GLU B 389 45.927 110.715 152.197 1.00 54.81 2031 O GLU B 389 45.401 110.088 151.280 1.00 91.54 2032 N GLU B 390 46.345 110.143 153.321 1.00 39.47 2033 CA GLU B 390 46.227 108.705 153.522 1.00 78.09 2034 CB GLU B 390 47.466 108.168 154.252 1.00 97.18 2035 CG GLU B 390 48.812 108.585 153.679 1.00 148.70 2036 CD GLU B 390 49.982 107.940 154.417 1.00 168.33 2037 OE1 GLU B 390 50.020 108.020 155.666 1.00 162.95 2038 OE2 GLU B 390 50.866 107.358 153.747 1.00 166.90 2039 C GLU B 390 45.000 108.231 154.301 1.00 24.57 2040 O GLU B 390 44.928 108.435 155.504 1.00 58.87 2041 N LYS B 391 44.046 107.581 153.638 1.00 39.47 2042 CA LYS B 391 42.892 107.033 154.357 1.00 36.12 2043 CB LYS B 391 41.939 106.319 153.392 1.00 30.68 2044 CG LYS B 391 40.901 105.431 154.103 1.00 91.41 2045 CD LYS B 391 40.563 104.141 153.322 1.00 153.55 2046 CE LYS B 391 39.785 104.403 152.029 1.00 171.40 2047 NZ LYS B 391 39.360 103.133 151.353 1.00 125.88 2048 C LYS B 391 43.471 106.004 155.342 1.00 35.98 2049 O LYS B 391 44.138 105.064 154.925 1.00 52.90 2050 N GLN B 392 43.232 106.173 156.636 1.00 47.33 2051 CA GLN B 392 43.778 105.248 157.617 1.00 50.54 2052 CB GLN B 392 44.026 105.955 158.932 1.00 52.52 2053 CG GLN B 392 44.910 107.158 158.819 1.00 43.19 2054 CD GLN B 392 46.307 106.799 158.433 1.00 52.17 2055 OE1 GLN B 392 46.549 106.342 157.315 1.00 140.45 2056 NE2 GLN B 392 47.251 106.987 159.354 1.00 104.37 2057 C GLN B 392 42.876 104.062 157.857 1.00 83.18 2058 O GLN B 392 41.730 104.057 157.421 1.00 48.10 2059 N ARG B 393 43.396 103.069 158.573 1.00 86.36 2060 CA ARG B 393 42.646 101.853 158.851 1.00 95.47 2061 CB ARG B 393 43.537 100.804 159.528 1.00 129.48 2062 CG ARG B 393 42.798 99.515 159.903 1.00 156.47 2063 CD ARG B 393 43.235 98.309 159.074 1.00 159.01 2064 NE ARG B 393 44.594 97.884 159.395 1.00 164.37 2065 CZ ARG B 393 45.164 96.782 158.918 1.00 170.49 2066 NH1 ARG B 393 44.492 95.988 158.094 1.00 168.61 2067 NH2 ARG B 393 46.408 96.474 159.267 1.00 175.65 2068 C ARG B 393 41.421 102.083 159.704 1.00 67.02 2069 O ARG B 393 40.379 101.483 159.461 1.00 85.39 2070 N ASN B 394 41.532 102.952 160.702 1.00 92.32 2071 CA ASN B 394 40.400 103.198 161.591 1.00 86.89 2072 CB ASN B 394 40.867 103.749 162.953 1.00 80.23 2073 CG ASN B 394 41.534 105.117 162.866 1.00 40.68 2074 OD1 ASN B 394 41.174 105.955 162.053 1.00 63.47 2075 ND2 ASN B 394 42.490 105.336 163.761 1.00 63.72 2076 C ASN B 394 39.286 104.073 161.044 1.00 37.93 2077 O ASN B 394 38.610 104.750 161.788 1.00 46.38 2078 N GLY B 395 39.075 104.048 159.740 1.00 70.31 2079 CA GLY B 395 38.004 104.853 159.177 1.00 65.82 2080 C GLY B 395 38.289 106.338 159.044 1.00 31.15 2081 O GLY B 395 37.619 107.040 158.285 1.00 51.28 2082 N THR B 396 39.286 106.822 159.774 1.00 53.28 2083 CA THR B 396 39.642 108.226 159.712 1.00 40.78 2084 CB THR B 396 40.600 108.599 160.829 1.00 19.53 2085 OG1 THR B 396 40.696 110.023 160.904 1.00 154.97 2086 CG2 THR B 396 41.976 108.064 160.557 1.00 109.19 2087 C THR B 396 40.296 108.573 158.383 1.00 40.28 2088 O THR B 396 40.205 107.818 157.422 1.00 73.66 2089 N LEU B 397 40.965 109.719 158.342 1.00 34.73 2090 CA LEU B 397 41.643 110.210 157.146 1.00 43.25 2091 CB LEU B 397 40.643 110.871 156.211 1.00 57.03 2092 CG LEU B 397 41.194 111.797 155.133 1.00 45.14 2093 CD1 LEU B 397 42.136 111.032 154.228 1.00 110.61 2094 CD2 LEU B 397 40.032 112.353 154.322 1.00 106.87 2095 C LEU B 397 42.678 111.231 157.579 1.00 52.48 2096 O LEU B 397 42.351 112.181 158.271 1.00 67.73 2097 N THR B 398 43.925 111.027 157.166 1.00 62.48 2098 CA THR B 398 45.033 111.910 157.522 1.00 36.96 2099 CB THR B 398 46.226 111.106 158.025 1.00 17.60 2100 OG1 THR B 398 45.893 110.477 159.258 1.00 49.11 2101 CG2 THR B 398 47.409 111.998 158.248 1.00 64.17 2102 C THR B 398 45.524 112.775 156.373 1.00 32.07 2103 O THR B 398 45.349 112.449 155.208 1.00 60.40 2104 N VAL B 399 46.156 113.882 156.725 1.00 24.42 2105 CA VAL B 399 46.695 114.800 155.749 1.00 35.05 2106 CB VAL B 399 45.788 116.004 155.569 1.00 18.51 2107 CG1 VAL B 399 46.501 117.089 154.798 1.00 27.22 2108 CG2 VAL B 399 44.534 115.572 154.853 1.00 29.70 2109 C VAL B 399 48.011 115.300 156.268 1.00 43.68 2110 O VAL B 399 48.063 115.809 157.380 1.00 42.74 2111 N THR B 400 49.082 115.139 155.495 1.00 53.46 2112 CA THR B 400 50.377 115.663 155.927 1.00 43.16 2113 CB THR B 400 51.450 114.598 156.085 1.00 42.86 2114 OG1 THR B 400 51.697 114.011 154.813 1.00 69.60 2115 CG2 THR B 400 51.014 113.532 157.036 1.00 42.99 2116 C THR B 400 50.862 116.598 154.844 1.00 51.26 2117 O THR B 400 50.595 116.382 153.656 1.00 66.11 2118 N SER B 401 51.573 117.637 155.261 1.00 47.73 2119 CA SER B 401 52.117 118.610 154.333 1.00 44.60 2120 CB SER B 401 51.199 119.817 154.209 1.00 50.71 2121 OG SER B 401 51.810 120.856 153.475 1.00 40.79 2122 C SER B 401 53.457 119.052 154.862 1.00 58.39 2123 O SER B 401 53.551 119.546 155.993 1.00 37.36 2124 N THR B 402 54.495 118.859 154.048 1.00 77.89 2125 CA THR B 402 55.840 119.241 154.442 1.00 61.20 2126 CB THR B 402 56.821 118.125 154.152 1.00 61.85 2127 OG1 THR B 402 56.295 116.895 154.661 1.00 81.37 2128 CG2 THR B 402 58.157 118.409 154.814 1.00 109.89 2129 C THR B 402 56.242 120.481 153.672 1.00 68.43 2130 O THR B 402 55.879 120.648 152.496 1.00 56.79 2131 N LEU B 403 56.991 121.354 154.339 1.00 62.35 2132 CA LEU B 403 57.413 122.599 153.719 1.00 65.76 2133 CB LEU B 403 56.613 123.752 154.320 1.00 66.45 2134 CG LEU B 403 56.909 125.152 153.790 1.00 75.07 2135 CD1 LEU B 403 56.506 125.263 152.324 1.00 107.93 2136 CD2 LEU B 403 56.167 126.156 154.629 1.00 75.06 2137 C LEU B 403 58.912 122.897 153.838 1.00 92.32 2138 O LEU B 403 59.488 122.821 154.932 1.00 34.92 2139 N PRO B 404 59.556 123.238 152.702 1.00 49.08 2140 CD PRO B 404 58.975 123.180 151.351 1.00 61.61 2141 CA PRO B 404 60.976 123.560 152.621 1.00 52.97 2142 CB PRO B 404 61.220 123.656 151.121 1.00 111.63 2143 CG PRO B 404 60.157 122.787 150.539 1.00 84.92 2144 C PRO B 404 61.217 124.891 153.310 1.00 73.53 2145 O PRO B 404 60.473 125.843 153.112 1.00 63.87 2146 N VAL B 405 62.282 124.975 154.087 1.00 86.35 2147 CA VAL B 405 62.543 126.198 154.812 1.00 76.26 2148 CB VAL B 405 62.100 126.000 156.269 1.00 36.70 2149 CG1 VAL B 405 63.203 126.416 157.230 1.00 127.12 2150 CG2 VAL B 405 60.845 126.775 156.513 1.00 88.70 2151 C VAL B 405 63.982 126.712 154.754 1.00 107.63 2152 O VAL B 405 64.940 125.951 154.939 1.00 91.98 2153 N GLY B 406 64.113 128.017 154.509 1.00 73.83 2154 CA GLY B 406 65.427 128.645 154.435 1.00 131.05 2155 C GLY B 406 66.225 128.509 155.736 1.00 130.39 2156 O GLY B 406 65.896 129.124 156.744 1.00 100.56 2157 N THR B 407 67.292 127.716 155.688 1.00 142.82 2158 CA THR B 407 68.143 127.461 156.830 1.00 100.01 2159 CB THR B 407 69.482 126.859 156.428 1.00 126.91 2160 OG1 THR B 407 69.350 126.170 155.184 1.00 151.73 2161 CG2 THR B 407 69.964 125.900 157.521 1.00 85.87 2162 C THR B 407 68.488 128.714 157.631 1.00 111.52 2163 O THR B 407 68.563 128.679 158.858 1.00 92.93 2164 N ARG B 408 68.734 129.816 156.934 1.00 135.67 2165 CA ARG B 408 69.098 131.063 157.590 1.00 137.76 2166 CB ARG B 408 69.517 132.097 156.546 1.00 153.22 2167 CG ARG B 408 70.749 131.688 155.715 1.00 174.72 2168 CD ARG B 408 70.530 130.402 154.906 1.00 170.05 2169 NE ARG B 408 69.575 130.568 153.813 1.00 157.68 2170 CZ ARG B 408 69.164 129.575 153.031 1.00 144.79 2171 NH1 ARG B 408 69.617 128.342 153.226 1.00 99.09 2172 NH2 ARG B 408 68.314 129.818 152.043 1.00 134.60 2173 C ARG B 408 67.905 131.589 158.374 1.00 125.74 2174 O ARG B 408 67.885 131.590 159.622 1.00 107.88 2175 N ASP B 409 66.897 132.018 157.626 1.00 114.38 2176 CA ASP B 409 65.665 132.577 158.171 1.00 100.02 2177 CB ASP B 409 64.547 132.393 157.129 1.00 106.65 2178 CG ASP B 409 64.925 132.915 155.743 1.00 131.77 2179 OD1 ASP B 409 64.961 134.151 155.545 1.00 128.42 2180 OD2 ASP B 409 65.187 132.086 154.841 1.00 107.93 2181 C ASP B 409 65.242 131.954 159.503 1.00 87.73 2182 O ASP B 409 64.932 132.667 160.459 1.00 125.50 2183 N TRP B 410 65.229 130.626 159.553 1.00 82.03 2184 CA TRP B 410 64.836 129.888 160.749 1.00 68.60 2185 CB TRP B 410 64.923 128.385 160.486 1.00 79.72 2186 CG TRP B 410 64.743 127.540 161.706 1.00 47.85 2187 CD2 TRP B 410 63.509 127.028 162.201 1.00 87.88 2188 CE2 TRP B 410 63.796 126.300 163.380 1.00 73.32 2189 CE3 TRP B 410 62.184 127.117 161.764 1.00 50.59 2190 CD1 TRP B 410 65.711 127.116 162.577 1.00 100.57 2191 NE1 TRP B 410 65.147 126.367 163.587 1.00 53.96 2192 CZ2 TRP B 410 62.806 125.668 164.127 1.00 90.94 2193 CZ3 TRP B 410 61.203 126.490 162.505 1.00 42.94 2194 CH2 TRP B 410 61.517 125.773 163.678 1.00 64.03 2195 C TRP B 410 65.675 130.226 161.960 1.00 98.97 2196 O TRP B 410 65.141 130.650 162.976 1.00 129.24 2197 N ILE B 411 66.985 130.031 161.860 1.00 106.60 2198 CA ILE B 411 67.850 130.306 162.998 1.00 115.95 2199 CB ILE B 411 69.317 130.062 162.670 1.00 103.18 2200 CG2 ILE B 411 70.075 129.721 163.955 1.00 112.78 2201 CG1 ILE B 411 69.438 128.905 161.683 1.00 127.25 2202 CD1 ILE B 411 70.843 128.694 161.174 1.00 162.43 2203 C ILE B 411 67.701 131.744 163.459 1.00 130.64 2204 O ILE B 411 67.892 132.055 164.637 1.00 115.79 2205 N GLU B 412 67.359 132.627 162.529 1.00 89.59 2206 CA GLU B 412 67.183 134.023 162.883 1.00 115.46 2207 CB GLU B 412 67.480 134.912 161.677 1.00 137.38 2208 CG GLU B 412 68.974 135.047 161.407 1.00 156.60 2209 CD GLU B 412 69.283 136.016 160.288 1.00 185.08 2210 OE1 GLU B 412 68.761 137.150 160.329 1.00 188.44 2211 OE2 GLU B 412 70.051 135.648 159.374 1.00 188.13 2212 C GLU B 412 65.799 134.316 163.458 1.00 140.17 2213 O GLU B 412 65.262 135.411 163.299 1.00 136.77 2214 N GLY B 413 65.228 133.314 164.121 1.00 164.88 2215 CA GLY B 413 63.931 133.461 164.761 1.00 159.55 2216 C GLY B 413 62.653 133.570 163.947 1.00 139.70 2217 O GLY B 413 61.592 133.808 164.523 1.00 138.95 2218 N GLU B 414 62.720 133.404 162.631 1.00 131.17 2219 CA GLU B 414 61.509 133.499 161.824 1.00 96.50 2220 CB GLU B 414 61.778 133.066 160.389 1.00 107.97 2221 CG GLU B 414 60.530 132.974 159.525 1.00 80.41 2222 CD GLU B 414 59.820 134.291 159.380 1.00 87.05 2223 OE1 GLU B 414 59.242 134.775 160.373 1.00 111.31 2224 OE2 GLU B 414 59.847 134.849 158.265 1.00 93.50 2225 C GLU B 414 60.420 132.622 162.423 1.00 101.40 2226 O GLU B 414 60.687 131.784 163.285 1.00 104.23 2227 N THR B 415 59.192 132.819 161.960 1.00 115.03 2228 CA THR B 415 58.056 132.059 162.458 1.00 112.22 2229 CB THR B 415 57.348 132.843 163.575 1.00 118.03 2230 OG1 THR B 415 55.994 132.403 163.687 1.00 110.64 2231 CG2 THR B 415 57.422 134.334 163.313 1.00 155.73 2232 C THR B 415 57.055 131.660 161.366 1.00 127.06 2233 O THR B 415 56.517 132.506 160.626 1.00 84.52 2234 N TYR B 416 56.818 130.351 161.282 1.00 115.33 2235 CA TYR B 416 55.922 129.765 160.287 1.00 76.98 2236 CB TYR B 416 56.626 128.606 159.569 1.00 86.80 2237 CG TYR B 416 57.961 128.956 158.940 1.00 94.67 2238 CD1 TYR B 416 59.155 128.835 159.662 1.00 110.20 2239 CE1 TYR B 416 60.380 129.198 159.099 1.00 47.43 2240 CD2 TYR B 416 58.024 129.446 157.635 1.00 61.95 2241 CE2 TYR B 416 59.231 129.815 157.066 1.00 64.97 2242 CZ TYR B 416 60.408 129.693 157.797 1.00 90.31 2243 OH TYR B 416 61.601 130.081 157.222 1.00 162.34 2244 C TYR B 416 54.623 129.255 160.897 1.00 92.23 2245 O TYR B 416 54.604 128.778 162.041 1.00 59.60 2246 N GLN B 417 53.546 129.322 160.115 1.00 62.55 2247 CA GLN B 417 52.236 128.889 160.592 1.00 50.69 2248 CB GLN B 417 51.411 130.114 160.969 1.00 129.83 2249 CG GLN B 417 50.127 129.811 161.708 1.00 147.33 2250 CD GLN B 417 49.282 131.051 161.924 1.00 140.76 2251 OE1 GLN B 417 48.740 131.624 160.971 1.00 120.92 2252 NE2 GLN B 417 49.167 131.477 163.181 1.00 129.75 2253 C GLN B 417 51.457 128.058 159.575 1.00 59.75 2254 O GLN B 417 51.437 128.363 158.381 1.00 76.03 2255 N CYS B 418 50.796 127.018 160.080 1.00 69.24 2256 CA CYS B 418 49.998 126.095 159.267 1.00 63.48 2257 C CYS B 418 48.521 126.354 159.532 1.00 71.26 2258 O CYS B 418 48.083 126.288 160.688 1.00 66.93 2259 CB CYS B 418 50.343 124.647 159.636 1.00 83.48 2260 SG CYS B 418 49.465 123.360 158.682 1.00 121.42 2261 N ARG B 419 47.756 126.640 158.474 1.00 40.08 2262 CA ARG B 419 46.327 126.928 158.637 1.00 38.15 2263 CB ARG B 419 46.008 128.369 158.211 1.00 106.47 2264 CG ARG B 419 44.562 128.797 158.483 1.00 184.87 2265 CD ARG B 419 44.235 130.164 157.902 1.00 224.39 2266 NE ARG B 419 42.880 130.587 158.248 1.00 235.46 2267 CZ ARG B 419 42.299 131.685 157.782 1.00 221.27 2268 NH1 ARG B 419 42.952 132.475 156.945 1.00 212.86 2269 NH2 ARG B 419 41.067 131.995 158.156 1.00 204.55 2270 C ARG B 419 45.434 125.975 157.868 1.00 66.29 2271 O ARG B 419 45.318 126.081 156.658 1.00 49.15 2272 N VAL B 420 44.777 125.056 158.565 1.00 41.47 2273 CA VAL B 420 43.891 124.107 157.877 1.00 57.57 2274 CB VAL B 420 44.050 122.684 158.466 1.00 53.54 2275 CG1 VAL B 420 45.434 122.539 159.084 1.00 58.35 2276 CG2 VAL B 420 42.980 122.416 159.517 1.00 71.65 2277 C VAL B 420 42.439 124.602 158.000 1.00 50.86 2278 O VAL B 420 42.085 125.213 159.020 1.00 51.31 2279 N THR B 421 41.636 124.307 156.966 1.00 31.63 2280 CA THR B 421 40.259 124.752 156.844 1.00 41.77 2281 CB THR B 421 40.214 126.119 156.170 1.00 12.47 2282 OG1 THR B 421 40.364 127.127 157.168 1.00 107.15 2283 CG2 THR B 421 38.907 126.314 155.393 1.00 70.23 2284 C THR B 421 39.294 123.902 156.029 1.00 49.50 2285 O THR B 421 39.438 123.788 154.818 1.00 60.59 2286 N HIS B 422 38.259 123.357 156.640 1.00 61.87 2287 CA HIS B 422 37.333 122.547 155.856 1.00 46.82 2288 CB HIS B 422 37.688 121.069 156.046 1.00 54.88 2289 CG HIS B 422 36.899 120.137 155.186 1.00 66.28 2290 CD2 HIS B 422 36.786 120.023 153.852 1.00 90.39 2291 ND1 HIS B 422 36.142 119.123 155.730 1.00 105.82 2292 CE1 HIS B 422 35.595 118.426 154.754 1.00 67.94 2293 NE2 HIS B 422 35.968 118.950 153.598 1.00 89.25 2294 C HIS B 422 35.883 122.789 156.278 1.00 35.50 2295 O HIS B 422 35.615 123.100 157.427 1.00 63.71 2296 N PRO B 423 34.938 122.661 155.333 1.00 33.86 2297 CD PRO B 423 35.231 122.574 153.889 1.00 61.95 2298 CA PRO B 423 33.500 122.844 155.563 1.00 74.49 2299 CB PRO B 423 32.892 122.227 154.320 1.00 30.75 2300 CG PRO B 423 33.833 122.723 153.266 1.00 92.20 2301 C PRO B 423 33.024 122.170 156.843 1.00 25.99 2302 O PRO B 423 32.254 122.745 157.604 1.00 94.74 2303 N HIS B 424 33.489 120.951 157.078 1.00 72.49 2304 CA HIS B 424 33.139 120.178 158.262 1.00 35.64 2305 CB HIS B 424 33.886 118.850 158.263 1.00 68.85 2306 CG HIS B 424 33.378 117.865 157.264 1.00 33.77 2307 CD2 HIS B 424 32.613 118.022 156.163 1.00 93.93 2308 ND1 HIS B 424 33.632 116.516 157.368 1.00 22.18 2309 CE1 HIS B 424 33.043 115.883 156.373 1.00 72.12 2310 NE2 HIS B 424 32.417 116.774 155.626 1.00 92.83 2311 C HIS B 424 33.562 120.919 159.503 1.00 72.43 2312 O HIS B 424 33.155 120.583 160.614 1.00 45.64 2313 N LEU B 425 34.397 121.925 159.310 1.00 30.28 2314 CA LEU B 425 34.907 122.679 160.429 1.00 67.62 2315 CB LEU B 425 36.415 122.774 160.284 1.00 51.81 2316 CG LEU B 425 37.061 121.393 160.189 1.00 50.51 2317 CD1 LEU B 425 38.563 121.538 160.155 1.00 99.40 2318 CD2 LEU B 425 36.651 120.562 161.377 1.00 41.28 2319 C LEU B 425 34.323 124.059 160.708 1.00 63.27 2320 O LEU B 425 34.105 124.859 159.800 1.00 102.78 2321 N PRO B 426 34.071 124.348 161.994 1.00 57.60 2322 CD PRO B 426 34.288 123.365 163.068 1.00 65.15 2323 CA PRO B 426 33.523 125.589 162.550 1.00 52.46 2324 CB PRO B 426 33.167 125.178 163.965 1.00 85.27 2325 CG PRO B 426 34.270 124.230 164.292 1.00 34.92 2326 C PRO B 426 34.576 126.710 162.531 1.00 49.56 2327 O PRO B 426 34.524 127.605 161.692 1.00 85.61 2328 N ARG B 427 35.513 126.657 163.475 1.00 56.31 2329 CA ARG B 427 36.606 127.626 163.550 1.00 81.37 2330 CB ARG B 427 37.101 127.788 165.016 1.00 37.35 2331 CG ARG B 427 37.494 126.478 165.701 1.00 67.67 2332 CD ARG B 427 37.021 126.334 167.163 1.00 106.61 2333 NE ARG B 427 36.476 124.989 167.420 1.00 156.12 2334 CZ ARG B 427 36.257 124.464 168.627 1.00 157.58 2335 NH1 ARG B 427 36.543 125.167 169.717 1.00 155.60 2336 NH2 ARG B 427 35.737 123.236 168.748 1.00 66.93 2337 C ARG B 427 37.709 127.037 162.664 1.00 71.40 2338 O ARG B 427 37.641 125.876 162.279 1.00 38.48 2339 N ALA B 428 38.713 127.824 162.313 1.00 105.95 2340 CA ALA B 428 39.793 127.289 161.495 1.00 47.56 2341 CB ALA B 428 40.458 128.403 160.734 1.00 123.77 2342 C ALA B 428 40.782 126.651 162.451 1.00 60.43 2343 O ALA B 428 40.721 126.891 163.651 1.00 68.94 2344 N LEU B 429 41.689 125.836 161.932 1.00 64.23 2345 CA LEU B 429 42.698 125.194 162.769 1.00 63.17 2346 CB LEU B 429 42.750 123.697 162.523 1.00 33.26 2347 CG LEU B 429 42.661 122.872 163.803 1.00 88.80 2348 CD1 LEU B 429 42.937 121.426 163.444 1.00 60.45 2349 CD2 LEU B 429 43.645 123.380 164.857 1.00 119.69 2350 C LEU B 429 44.041 125.779 162.418 1.00 60.60 2351 O LEU B 429 44.392 125.847 161.247 1.00 46.41 2352 N MET B 430 44.792 126.186 163.433 1.00 45.54 2353 CA MET B 430 46.085 126.789 163.209 1.00 42.39 2354 CB MET B 430 46.004 128.321 163.336 1.00 51.46 2355 CG MET B 430 45.156 129.011 162.277 1.00 72.95 2356 SD MET B 430 45.247 130.811 162.351 1.00 135.30 2357 CE MET B 430 44.061 131.159 163.665 1.00 161.36 2358 C MET B 430 47.063 126.286 164.226 1.00 61.09 2359 O MET B 430 46.686 125.890 165.335 1.00 52.58 2360 N ARG B 431 48.326 126.285 163.821 1.00 42.23 2361 CA ARG B 431 49.423 125.906 164.696 1.00 63.07 2362 CB ARG B 431 49.602 124.404 164.736 1.00 33.42 2363 CG ARG B 431 48.302 123.660 164.986 1.00 57.91 2364 CD ARG B 431 48.510 122.413 165.816 1.00 51.62 2365 NE ARG B 431 48.125 122.644 167.201 1.00 93.78 2366 CZ ARG B 431 46.876 122.871 167.585 1.00 101.45 2367 NH1 ARG B 431 45.907 122.888 166.681 1.00 36.13 2368 NH2 ARG B 431 46.601 123.088 168.865 1.00 161.49 2369 C ARG B 431 50.627 126.588 164.085 1.00 72.59 2370 O ARG B 431 50.663 126.820 162.869 1.00 53.93 2371 N SER B 432 51.589 126.941 164.928 1.00 70.72 2372 CA SER B 432 52.772 127.634 164.457 1.00 71.54 2373 CB SER B 432 52.625 129.138 164.671 1.00 72.40 2374 OG SER B 432 52.566 129.443 166.058 1.00 106.30 2375 C SER B 432 53.974 127.142 165.224 1.00 99.13 2376 O SER B 432 53.831 126.433 166.226 1.00 55.86 2377 N THR B 433 55.155 127.529 164.749 1.00 84.30 2378 CA THR B 433 56.400 127.130 165.384 1.00 88.35 2379 CB THR B 433 56.722 125.683 165.096 1.00 76.49 2380 OG1 THR B 433 57.898 125.303 165.820 1.00 105.68 2381 CG2 THR B 433 56.953 125.506 163.607 1.00 49.60 2382 C THR B 433 57.567 127.947 164.891 1.00 97.22 2383 O THR B 433 57.576 128.410 163.734 1.00 66.32 2384 N THR B 434 58.546 128.111 165.785 1.00 77.69 2385 CA THR B 434 59.786 128.838 165.511 1.00 65.57 2386 CB THR B 434 59.687 130.335 165.820 1.00 84.37 2387 OG1 THR B 434 59.875 130.555 167.229 1.00 140.54 2388 CG2 THR B 434 58.342 130.886 165.421 1.00 65.31 2389 C THR B 434 60.880 128.307 166.436 1.00 96.20 2390 O THR B 434 60.621 127.548 167.360 1.00 67.43 2391 N LYS B 435 62.095 128.750 166.146 1.00 102.83 2392 CA LYS B 435 63.296 128.401 166.859 1.00 94.54 2393 CB LYS B 435 64.392 129.385 166.468 1.00 102.66 2394 CG LYS B 435 65.736 129.328 167.181 1.00 156.34 2395 CD LYS B 435 66.662 130.374 166.492 1.00 155.89 2396 CE LYS B 435 68.100 130.543 167.040 1.00 174.55 2397 NZ LYS B 435 68.097 131.005 168.483 1.00 180.88 2398 C LYS B 435 63.073 128.443 168.369 1.00 90.68 2399 O LYS B 435 62.554 129.421 168.898 1.00 125.40 2400 N THR B 436 63.449 127.383 169.070 1.00 65.76 2401 CA THR B 436 63.293 127.351 170.526 1.00 80.29 2402 CB THR B 436 63.710 126.002 171.078 1.00 74.52 2403 OG1 THR B 436 63.054 124.968 170.344 1.00 133.68 2404 CG2 THR B 436 63.341 125.879 172.532 1.00 84.46 2405 C THR B 436 64.159 128.429 171.186 1.00 132.09 2406 O THR B 436 65.294 128.670 170.764 1.00 135.39 2407 N SER B 437 63.639 129.031 172.255 1.00 135.64 2408 CA SER B 437 64.341 130.112 172.957 1.00 154.94 2409 CB SER B 437 63.334 131.187 173.370 1.00 159.96 2410 OG SER B 437 62.326 130.634 174.204 1.00 151.19 2411 C SER B 437 65.157 129.701 174.176 1.00 145.96 2412 O SER B 437 65.253 128.518 174.505 1.00 126.88 2413 N GLY B 438 65.748 130.698 174.834 1.00 142.79 2414 CA GLY B 438 66.544 130.446 176.022 1.00 127.41 2415 C GLY B 438 68.046 130.551 175.823 1.00 105.05 2416 O GLY B 438 68.511 131.074 174.814 1.00 92.39 2417 N PRO B 439 68.836 130.081 176.796 1.00 96.54 2418 CD PRO B 439 68.372 129.693 178.137 1.00 102.85 2419 CA PRO B 439 70.299 130.103 176.748 1.00 119.07 2420 CB PRO B 439 70.684 130.075 178.218 1.00 146.55 2421 CG PRO B 439 69.637 129.177 178.787 1.00 118.33 2422 C PRO B 439 70.807 128.876 175.989 1.00 126.07 2423 O PRO B 439 70.310 127.768 176.199 1.00 134.45 2424 N ARG B 440 71.805 129.094 175.127 1.00 120.46 2425 CA ARG B 440 72.374 128.039 174.291 1.00 111.19 2426 CB ARG B 440 72.576 128.565 172.866 1.00 122.47 2427 CG ARG B 440 71.504 129.538 172.390 1.00 147.23 2428 CD ARG B 440 70.181 128.851 172.101 1.00 186.68 2429 NE ARG B 440 69.065 129.796 172.154 1.00 214.53 2430 CZ ARG B 440 67.972 129.726 171.400 1.00 221.94 2431 NH1 ARG B 440 67.829 128.750 170.511 1.00 219.20 2432 NH2 ARG B 440 67.023 130.642 171.541 1.00 205.02 2433 C ARG B 440 73.699 127.481 174.812 1.00 89.64 2434 O ARG B 440 74.753 128.090 174.628 1.00 132.22 2435 N ALA B 441 73.650 126.315 175.450 1.00 73.11 2436 CA ALA B 441 74.869 125.692 175.965 1.00 83.71 2437 CB ALA B 441 74.701 125.340 177.430 1.00 94.78 2438 C ALA B 441 75.217 124.441 175.151 1.00 85.35 2439 O ALA B 441 74.409 123.514 175.047 1.00 93.65 2440 N ALA B 442 76.430 124.427 174.595 1.00 115.97 2441 CA ALA B 442 76.938 123.321 173.775 1.00 86.76 2442 CB ALA B 442 78.341 123.654 173.274 1.00 132.70 2443 C ALA B 442 76.946 121.954 174.466 1.00 93.35 2444 O ALA B 442 76.879 121.858 175.693 1.00 88.94 2445 N PRO B 443 77.045 120.877 173.670 1.00 88.73 2446 CD PRO B 443 76.967 120.894 172.202 1.00 53.59 2447 CA PRO B 443 77.057 119.497 174.160 1.00 66.28 2448 CB PRO B 443 76.504 118.696 172.982 1.00 75.52 2449 CG PRO B 443 76.059 119.745 171.951 1.00 82.83 2450 C PRO B 443 78.413 118.970 174.561 1.00 69.00 2451 O PRO B 443 79.442 119.348 174.008 1.00 107.52 2452 N GLU B 444 78.391 118.073 175.529 1.00 79.76 2453 CA GLU B 444 79.594 117.429 176.022 1.00 111.19 2454 CB GLU B 444 79.710 117.589 177.542 1.00 148.56 2455 CG GLU B 444 80.142 118.972 178.015 1.00 175.46 2456 CD GLU B 444 79.828 119.211 179.486 1.00 159.46 2457 OE1 GLU B 444 79.978 118.265 180.292 1.00 128.82 2458 OE2 GLU B 444 79.438 120.349 179.836 1.00 148.10 2459 C GLU B 444 79.351 115.976 175.686 1.00 93.99 2460 O GLU B 444 78.357 115.406 176.121 1.00 102.87 2461 N VAL B 445 80.235 115.375 174.903 1.00 98.05 2462 CA VAL B 445 80.056 113.978 174.543 1.00 82.80 2463 CB VAL B 445 79.787 113.845 173.042 1.00 75.64 2464 CG1 VAL B 445 80.696 114.770 172.266 1.00 56.15 2465 CG2 VAL B 445 79.983 112.403 172.620 1.00 100.09 2466 C VAL B 445 81.230 113.081 174.936 1.00 52.47 2467 O VAL B 445 82.385 113.474 174.820 1.00 84.33 2468 N TYR B 446 80.917 111.877 175.406 1.00 58.93 2469 CA TYR B 446 81.928 110.913 175.817 1.00 94.16 2470 CB TYR B 446 82.051 110.897 177.344 1.00 114.12 2471 CG TYR B 446 82.132 112.276 177.967 1.00 123.21 2472 CD1 TYR B 446 81.042 112.826 178.628 1.00 107.03 2473 CE1 TYR B 446 81.091 114.111 179.161 1.00 140.23 2474 CD2 TYR B 446 83.288 113.048 177.854 1.00 175.76 2475 CE2 TYR B 446 83.347 114.338 178.384 1.00 166.71 2476 CZ TYR B 446 82.242 114.861 179.034 1.00 148.92 2477 OH TYR B 446 82.281 116.137 179.545 1.00 163.80 2478 C TYR B 446 81.515 109.532 175.325 1.00 98.27 2479 O TYR B 446 80.467 109.032 175.715 1.00 94.14 2480 N ALA B 447 82.337 108.917 174.476 1.00 102.60 2481 CA ALA B 447 82.035 107.592 173.925 1.00 60.72 2482 CB ALA B 447 82.452 107.548 172.479 1.00 85.56 2483 C ALA B 447 82.706 106.451 174.698 1.00 79.19 2484 O ALA B 447 83.836 106.585 175.166 1.00 86.10 2485 N PHE B 448 82.018 105.322 174.823 1.00 45.82 2486 CA PHE B 448 82.569 104.190 175.560 1.00 98.07 2487 CB PHE B 448 81.848 104.064 176.905 1.00 113.90 2488 CG PHE B 448 81.973 105.292 177.762 1.00 142.00 2489 CD1 PHE B 448 81.192 106.412 177.512 1.00 154.40 2490 CD2 PHE B 448 82.920 105.353 178.777 1.00 186.99 2491 CE1 PHE B 448 81.356 107.576 178.258 1.00 156.24 2492 CE2 PHE B 448 83.091 106.511 179.529 1.00 185.02 2493 CZ PHE B 448 82.309 107.625 179.268 1.00 183.09 2494 C PHE B 448 82.528 102.867 174.795 1.00 87.01 2495 O PHE B 448 82.229 102.854 173.608 1.00 104.18 2496 N ALA B 449 82.843 101.761 175.468 1.00 79.78 2497 CA ALA B 449 82.846 100.458 174.814 1.00 40.21 2498 CB ALA B 449 83.970 100.401 173.803 1.00 97.16 2499 C ALA B 449 82.959 99.284 175.780 1.00 54.65 2500 O ALA B 449 83.846 99.231 176.623 1.00 65.36 2501 N THR B 450 82.061 98.325 175.619 1.00 48.81 2502 CA THR B 450 81.993 97.144 176.467 1.00 85.23 2503 CB THR B 450 80.626 96.450 176.266 1.00 58.63 2504 OG1 THR B 450 79.578 97.340 176.657 1.00 98.59 2505 CG2 THR B 450 80.529 95.176 177.085 1.00 107.27 2506 C THR B 450 83.088 96.099 176.252 1.00 86.98 2507 O THR B 450 83.677 96.015 175.182 1.00 115.23 2508 N PRO B 451 83.398 95.317 177.298 1.00 82.22 2509 CD PRO B 451 83.248 95.823 178.669 1.00 78.05 2510 CA PRO B 451 84.401 94.247 177.274 1.00 102.30 2511 CB PRO B 451 84.895 94.197 178.715 1.00 127.73 2512 CG PRO B 451 84.606 95.567 179.233 1.00 117.16 2513 C PRO B 451 83.638 92.976 176.904 1.00 102.38 2514 O PRO B 451 82.434 92.893 177.140 1.00 107.16 2515 N GLU B 452 84.316 91.984 176.339 1.00 119.75 2516 CA GLU B 452 83.619 90.760 175.950 1.00 135.04 2517 CB GLU B 452 84.588 89.759 175.301 1.00 160.10 2518 CG GLU B 452 85.720 89.279 176.195 1.00 192.95 2519 CD GLU B 452 86.553 88.193 175.536 1.00 193.27 2520 OE1 GLU B 452 85.996 87.113 175.242 1.00 173.50 2521 OE2 GLU B 452 87.762 88.420 175.311 1.00 191.58 2522 C GLU B 452 82.901 90.097 177.120 1.00 120.59 2523 O GLU B 452 83.117 90.448 178.278 1.00 87.28 2524 N TRP B 453 82.040 89.138 176.797 1.00 120.79 2525 CA TRP B 453 81.274 88.403 177.793 1.00 141.89 2526 CB TRP B 453 79.909 89.074 177.986 1.00 165.76 2527 CG TRP B 453 78.970 88.353 178.913 1.00 194.36 2528 CD2 TRP B 453 78.780 88.606 180.312 1.00 210.98 2529 CE2 TRP B 453 77.810 87.688 180.773 1.00 213.28 2530 CE3 TRP B 453 79.338 89.515 181.221 1.00 215.87 2531 CD1 TRP B 453 78.130 87.324 178.595 1.00 204.35 2532 NE1 TRP B 453 77.429 86.920 179.705 1.00 205.41 2533 CZ2 TRP B 453 77.382 87.656 182.106 1.00 220.95 2534 CZ3 TRP B 453 78.913 89.483 182.547 1.00 216.68 2535 CH2 TRP B 453 77.945 88.557 182.975 1.00 222.83 2536 C TRP B 453 81.111 86.952 177.340 1.00 151.58 2537 O TRP B 453 80.894 86.679 176.161 1.00 148.39 2538 N PRO B 454 81.227 86.000 178.277 1.00 154.83 2539 CD PRO B 454 81.493 86.244 179.707 1.00 142.37 2540 CA PRO B 454 81.101 84.563 178.014 1.00 175.73 2541 CB PRO B 454 80.922 83.982 179.410 1.00 177.55 2542 CG PRO B 454 81.817 84.854 180.224 1.00 168.66 2543 C PRO B 454 79.962 84.171 177.075 1.00 189.74 2544 O PRO B 454 79.983 83.092 176.485 1.00 208.45 2545 N GLY B 455 78.971 85.045 176.945 1.00 196.85 2546 CA GLY B 455 77.842 84.759 176.078 1.00 187.96 2547 C GLY B 455 78.211 84.739 174.607 1.00 180.32 2548 O GLY B 455 77.762 83.871 173.859 1.00 192.44 2549 N SER B 456 79.029 85.701 174.192 1.00 169.42 2550 CA SER B 456 79.463 85.802 172.801 1.00 166.91 2551 CB SER B 456 78.471 86.631 171.992 1.00 158.61 2552 OG SER B 456 78.452 87.968 172.457 1.00 140.70 2553 C SER B 456 80.824 86.474 172.755 1.00 166.74 2554 O SER B 456 81.092 87.397 173.523 1.00 173.32 2555 N ARG B 457 81.677 86.022 171.844 1.00 174.22 2556 CA ARG B 457 83.016 86.582 171.723 1.00 176.54 2557 CB ARG B 457 84.057 85.452 171.727 1.00 182.95 2558 CG ARG B 457 83.970 84.538 172.946 1.00 199.86 2559 CD ARG B 457 85.036 83.449 172.934 1.00 203.45 2560 NE ARG B 457 84.881 82.538 174.067 1.00 215.80 2561 CZ ARG B 457 85.704 81.529 174.339 1.00 205.75 2562 NH1 ARG B 457 86.751 81.296 173.558 1.00 206.61 2563 NH2 ARG B 457 85.479 80.751 175.391 1.00 185.40 2564 C ARG B 457 83.180 87.431 170.468 1.00 160.43 2565 O ARG B 457 84.282 87.892 170.169 1.00 168.18 2566 N ASP B 458 82.090 87.647 169.737 1.00 145.98 2567 CA ASP B 458 82.161 88.438 168.512 1.00 164.53 2568 CB ASP B 458 82.048 87.527 167.289 1.00 187.11 2569 CG ASP B 458 83.221 86.575 167.162 1.00 204.04 2570 OD1 ASP B 458 84.377 87.051 167.162 1.00 205.31 2571 OD2 ASP B 458 82.989 85.352 167.062 1.00 200.56 2572 C ASP B 458 81.118 89.543 168.419 1.00 166.34 2573 O ASP B 458 80.827 90.043 167.329 1.00 100.86 2574 N LYS B 459 80.561 89.920 169.566 1.00 179.43 2575 CA LYS B 459 79.561 90.978 169.629 1.00 157.46 2576 CB LYS B 459 78.155 90.385 169.808 1.00 170.13 2577 CG LYS B 459 77.680 89.492 168.663 1.00 195.45 2578 CD LYS B 459 76.254 88.985 168.892 1.00 180.52 2579 CE LYS B 459 75.783 88.106 167.737 1.00 168.06 2580 NZ LYS B 459 74.380 87.632 167.911 1.00 140.21 2581 C LYS B 459 79.886 91.894 170.805 1.00 156.35 2582 O LYS B 459 79.922 91.450 171.953 1.00 165.29 2583 N ARG B 460 80.140 93.167 170.515 1.00 147.60 2584 CA ARG B 460 80.444 94.141 171.561 1.00 148.70 2585 CB ARG B 460 81.942 94.468 171.566 1.00 116.00 2586 CG ARG B 460 82.793 93.307 172.076 1.00 133.11 2587 CD ARG B 460 84.209 93.727 172.454 1.00 145.86 2588 NE ARG B 460 84.924 92.645 173.130 1.00 154.57 2589 CZ ARG B 460 86.106 92.776 173.728 1.00 176.49 2590 NH1 ARG B 460 86.723 93.949 173.741 1.00 156.00 2591 NH2 ARG B 460 86.673 91.733 174.320 1.00 195.46 2592 C ARG B 460 79.595 95.410 171.423 1.00 134.14 2593 O ARG B 460 79.384 95.915 170.320 1.00 108.53 2594 N THR B 461 79.124 95.914 172.562 1.00 97.76 2595 CA THR B 461 78.240 97.078 172.631 1.00 80.21 2596 CB THR B 461 77.224 96.860 173.750 1.00 88.28 2597 OG1 THR B 461 76.775 95.499 173.711 1.00 112.83 2598 CG2 THR B 461 76.037 97.804 173.597 1.00 61.89 2599 C THR B 461 78.845 98.467 172.849 1.00 76.50 2600 O THR B 461 79.691 98.647 173.719 1.00 62.71 2601 N LEU B 462 78.385 99.453 172.079 1.00 66.18 2602 CA LEU B 462 78.869 100.827 172.229 1.00 94.33 2603 CB LEU B 462 79.268 101.446 170.885 1.00 67.03 2604 CG LEU B 462 80.510 100.946 170.147 1.00 85.83 2605 CD1 LEU B 462 81.004 102.049 169.214 1.00 60.23 2606 CD2 LEU B 462 81.594 100.578 171.134 1.00 69.11 2607 C LEU B 462 77.811 101.721 172.867 1.00 93.33 2608 O LEU B 462 76.612 101.466 172.742 1.00 137.10 2609 N ALA B 463 78.267 102.777 173.538 1.00 84.75 2610 CA ALA B 463 77.385 103.730 174.207 1.00 57.78 2611 CB ALA B 463 77.231 103.369 175.655 1.00 67.02 2612 C ALA B 463 77.982 105.115 174.089 1.00 65.49 2613 O ALA B 463 79.197 105.283 174.138 1.00 79.68 2614 N CYS B 464 77.127 106.114 173.950 1.00 77.94 2615 CA CYS B 464 77.599 107.476 173.795 1.00 76.01 2616 C CYS B 464 76.707 108.413 174.573 1.00 97.04 2617 O CYS B 464 75.511 108.494 174.317 1.00 118.25 2618 CB CYS B 464 77.580 107.839 172.322 1.00 48.71 2619 SG CYS B 464 78.259 109.457 171.871 1.00 108.42 2620 N LEU B 465 77.300 109.120 175.526 1.00 104.12 2621 CA LEU B 465 76.568 110.055 176.368 1.00 83.50 2622 CB LEU B 465 76.945 109.819 177.827 1.00 57.15 2623 CG LEU B 465 76.704 110.946 178.820 1.00 72.22 2624 CD1 LEU B 465 75.332 111.558 178.626 1.00 80.58 2625 CD2 LEU B 465 76.872 110.378 180.214 1.00 78.64 2626 C LEU B 465 76.796 111.517 175.999 1.00 76.86 2627 O LEU B 465 77.918 111.999 175.967 1.00 62.37 2628 N ILE B 466 75.713 112.220 175.726 1.00 63.57 2629 CA ILE B 466 75.794 113.617 175.367 1.00 60.62 2630 CB ILE B 466 75.174 113.839 173.997 1.00 81.07 2631 CG2 ILE B 466 75.447 115.266 173.508 1.00 60.00 2632 CG1 ILE B 466 75.729 112.784 173.042 1.00 33.92 2633 CD1 ILE B 466 75.341 113.005 171.599 1.00 85.20 2634 C ILE B 466 75.029 114.398 176.420 1.00 93.44 2635 O ILE B 466 73.826 114.215 176.575 1.00 96.66 2636 N GLN B 467 75.723 115.271 177.142 1.00 102.53 2637 CA GLN B 467 75.072 116.033 178.195 1.00 81.78 2638 CB GLN B 467 75.418 115.422 179.552 1.00 45.68 2639 CG GLN B 467 76.895 115.224 179.783 1.00 79.30 2640 CD GLN B 467 77.217 114.845 181.222 1.00 113.12 2641 OE1 GLN B 467 76.587 113.958 181.809 1.00 73.47 2642 NE2 GLN B 467 78.213 115.514 181.794 1.00 129.90 2643 C GLN B 467 75.318 117.535 178.260 1.00 57.56 2644 O GLN B 467 75.964 118.136 177.400 1.00 58.32 2645 N ASN B 468 74.751 118.122 179.306 1.00 90.17 2646 CA ASN B 468 74.855 119.537 179.600 1.00 80.28 2647 CB ASN B 468 76.182 119.806 180.295 1.00 100.04 2648 CG ASN B 468 76.430 118.848 181.444 1.00 135.69 2649 OD1 ASN B 468 75.579 118.677 182.323 1.00 115.44 2650 ND2 ASN B 468 77.598 118.211 181.442 1.00 138.13 2651 C ASN B 468 74.695 120.436 178.395 1.00 92.36 2652 O ASN B 468 75.553 121.266 178.104 1.00 115.17 2653 N PHE B 469 73.582 120.273 177.696 1.00 53.18 2654 CA PHE B 469 73.314 121.103 176.537 1.00 71.01 2655 CB PHE B 469 73.459 120.295 175.246 1.00 56.66 2656 CG PHE B 469 72.531 119.107 175.155 1.00 100.03 2657 CD1 PHE B 469 71.424 119.130 174.306 1.00 45.65 2658 CD2 PHE B 469 72.781 117.952 175.895 1.00 97.64 2659 CE1 PHE B 469 70.593 118.026 174.192 1.00 97.74 2660 CE2 PHE B 469 71.946 116.838 175.785 1.00 35.93 2661 CZ PHE B 469 70.855 116.877 174.934 1.00 100.21 2662 C PHE B 469 71.917 121.672 176.618 1.00 72.62 2663 O PHE B 469 71.106 121.247 177.450 1.00 57.82 2664 N MET B 470 71.650 122.640 175.748 1.00 28.09 2665 CA MET B 470 70.344 123.287 175.681 1.00 59.88 2666 CB MET B 470 70.018 123.983 177.000 1.00 109.60 2667 CG MET B 470 71.139 124.822 177.586 1.00 125.93 2668 SD MET B 470 71.008 124.868 179.393 1.00 132.45 2669 CE MET B 470 69.604 125.930 179.600 1.00 165.70 2670 C MET B 470 70.355 124.265 174.524 1.00 62.44 2671 O MET B 470 71.359 124.924 174.279 1.00 61.44 2672 N PRO B 471 69.224 124.398 173.803 1.00 78.95 2673 CD PRO B 471 69.191 125.344 172.677 1.00 80.51 2674 CA PRO B 471 67.936 123.696 173.918 1.00 80.70 2675 CB PRO B 471 67.159 124.210 172.709 1.00 74.00 2676 CG PRO B 471 67.714 125.581 172.516 1.00 99.60 2677 C PRO B 471 68.028 122.180 173.923 1.00 80.76 2678 O PRO B 471 69.116 121.612 173.879 1.00 103.67 2679 N GLU B 472 66.879 121.518 173.962 1.00 88.76 2680 CA GLU B 472 66.873 120.070 173.975 1.00 85.51 2681 CB GLU B 472 65.665 119.551 174.757 1.00 112.19 2682 CG GLU B 472 64.326 120.100 174.287 1.00 171.67 2683 CD GLU B 472 63.145 119.321 174.848 1.00 191.16 2684 OE1 GLU B 472 63.088 119.123 176.083 1.00 177.52 2685 OE2 GLU B 472 62.272 118.908 174.053 1.00 195.05 2686 C GLU B 472 66.878 119.472 172.575 1.00 108.68 2687 O GLU B 472 67.002 118.258 172.429 1.00 108.87 2688 N ASP B 473 66.748 120.310 171.548 1.00 67.19 2689 CA ASP B 473 66.747 119.812 170.168 1.00 94.32 2690 CB ASP B 473 66.278 120.901 169.206 1.00 108.16 2691 CG ASP B 473 64.829 121.247 169.396 1.00 130.25 2692 OD1 ASP B 473 64.004 120.313 169.448 1.00 152.46 2693 OD2 ASP B 473 64.511 122.446 169.486 1.00 127.62 2694 C ASP B 473 68.118 119.302 169.725 1.00 86.57 2695 O ASP B 473 69.002 120.089 169.380 1.00 76.15 2696 N ILE B 474 68.283 117.982 169.704 1.00 86.59 2697 CA ILE B 474 69.559 117.388 169.332 1.00 62.99 2698 CB ILE B 474 70.315 116.903 170.597 1.00 70.94 2699 CG2 ILE B 474 69.789 115.557 171.052 1.00 49.54 2700 CG1 ILE B 474 71.798 116.740 170.301 1.00 79.49 2701 CD1 ILE B 474 72.587 116.274 171.507 1.00 78.48 2702 C ILE B 474 69.446 116.217 168.360 1.00 81.03 2703 O ILE B 474 68.513 115.412 168.436 1.00 79.23 2704 N SER B 475 70.410 116.134 167.448 1.00 80.57 2705 CA SER B 475 70.478 115.057 166.464 1.00 72.68 2706 CB SER B 475 70.451 115.624 165.044 1.00 48.43 2707 OG SER B 475 69.152 115.552 164.488 1.00 90.69 2708 C SER B 475 71.758 114.239 166.657 1.00 52.82 2709 O SER B 475 72.857 114.708 166.371 1.00 78.59 2710 N VAL B 476 71.611 113.020 167.154 1.00 56.94 2711 CA VAL B 476 72.746 112.127 167.364 1.00 46.67 2712 CB VAL B 476 72.522 111.246 168.605 1.00 59.60 2713 CG1 VAL B 476 73.590 110.197 168.732 1.00 49.38 2714 CG2 VAL B 476 72.520 112.094 169.816 1.00 76.03 2715 C VAL B 476 72.884 111.219 166.133 1.00 66.33 2716 O VAL B 476 71.938 111.062 165.354 1.00 113.57 2717 N GLN B 477 74.065 110.632 165.961 1.00 72.08 2718 CA GLN B 477 74.340 109.725 164.850 1.00 86.67 2719 CB GLN B 477 74.256 110.474 163.530 1.00 59.98 2720 CG GLN B 477 75.039 111.750 163.500 1.00 52.42 2721 CD GLN B 477 74.806 112.507 162.215 1.00 113.14 2722 OE1 GLN B 477 73.664 112.831 161.874 1.00 115.80 2723 NE2 GLN B 477 75.884 112.792 161.487 1.00 104.02 2724 C GLN B 477 75.712 109.077 164.987 1.00 71.96 2725 O GLN B 477 76.433 109.318 165.946 1.00 72.78 2726 N TRP B 478 76.071 108.231 164.038 1.00 74.54 2727 CA TRP B 478 77.371 107.594 164.114 1.00 91.24 2728 CB TRP B 478 77.254 106.181 164.656 1.00 30.97 2729 CG TRP B 478 76.687 106.064 166.023 1.00 64.60 2730 CD2 TRP B 478 77.409 105.759 167.220 1.00 55.53 2731 CE2 TRP B 478 76.461 105.528 168.231 1.00 51.61 2732 CE3 TRP B 478 78.767 105.646 167.531 1.00 88.58 2733 CD1 TRP B 478 75.371 106.032 166.355 1.00 68.44 2734 NE1 TRP B 478 75.222 105.702 167.676 1.00 76.50 2735 CZ2 TRP B 478 76.824 105.184 169.534 1.00 99.88 2736 CZ3 TRP B 478 79.129 105.302 168.828 1.00 73.67 2737 CH2 TRP B 478 78.159 105.074 169.812 1.00 68.61 2738 C TRP B 478 78.063 107.529 162.771 1.00 73.34 2739 O TRP B 478 77.417 107.546 161.726 1.00 112.30 2740 N LEU B 479 79.387 107.450 162.811 1.00 54.55 2741 CA LEU B 479 80.171 107.362 161.597 1.00 75.53 2742 CB LEU B 479 80.982 108.634 161.420 1.00 86.60 2743 CG LEU B 479 80.135 109.894 161.606 1.00 64.71 2744 CD1 LEU B 479 81.024 111.119 161.500 1.00 143.30 2745 CD2 LEU B 479 79.031 109.939 160.564 1.00 91.15 2746 C LEU B 479 81.081 106.160 161.743 1.00 90.65 2747 O LEU B 479 81.316 105.695 162.856 1.00 67.67 2748 N HIS B 480 81.582 105.652 160.621 1.00 130.81 2749 CA HIS B 480 82.460 104.487 160.635 1.00 114.42 2750 CB HIS B 480 81.646 103.225 160.911 1.00 109.89 2751 CG HIS B 480 82.423 101.954 160.772 1.00 101.08 2752 CD2 HIS B 480 82.120 100.790 160.152 1.00 114.03 2753 ND1 HIS B 480 83.644 101.759 161.379 1.00 82.41 2754 CE1 HIS B 480 84.057 100.527 161.144 1.00 108.15 2755 NE2 HIS B 480 83.151 99.917 160.402 1.00 119.50 2756 C HIS B 480 83.186 104.348 159.316 1.00 84.59 2757 O HIS B 480 82.657 103.811 158.351 1.00 86.39 2758 N ASN B 481 84.406 104.846 159.275 1.00 93.11 2759 CA ASN B 481 85.181 104.760 158.059 1.00 118.77 2760 CB ASN B 481 85.276 103.302 157.612 1.00 96.52 2761 CG ASN B 481 86.518 103.023 156.817 1.00 137.81 2762 OD1 ASN B 481 86.812 101.876 156.498 1.00 143.19 2763 ND2 ASN B 481 87.262 104.075 156.488 1.00 162.07 2764 C ASN B 481 84.527 105.608 156.973 1.00 70.50 2765 O ASN B 481 84.388 105.183 155.836 1.00 95.06 2766 N GLU B 482 84.126 106.814 157.345 1.00 75.74 2767 CA GLU B 482 83.512 107.746 156.415 1.00 123.11 2768 CB GLU B 482 84.424 107.940 155.198 1.00 121.91 2769 CG GLU B 482 85.873 108.306 155.542 1.00 142.86 2770 CD GLU B 482 86.012 109.651 156.248 1.00 171.49 2771 OE1 GLU B 482 85.641 110.686 155.650 1.00 170.24 2772 OE2 GLU B 482 86.497 109.672 157.401 1.00 170.99 2773 C GLU B 482 82.130 107.277 155.969 1.00 104.98 2774 O GLU B 482 81.647 107.661 154.902 1.00 66.15 2775 N VAL B 483 81.490 106.457 156.795 1.00 66.23 2776 CA VAL B 483 80.164 105.948 156.472 1.00 92.18 2777 CB VAL B 483 80.210 104.427 156.245 1.00 99.60 2778 CG1 VAL B 483 78.813 103.869 156.069 1.00 96.51 2779 CG2 VAL B 483 81.050 104.125 155.022 1.00 173.41 2780 C VAL B 483 79.140 106.250 157.562 1.00 113.67 2781 O VAL B 483 79.184 105.661 158.640 1.00 139.78 2782 N GLN B 484 78.214 107.164 157.276 1.00 105.77 2783 CA GLN B 484 77.165 107.533 158.231 1.00 69.76 2784 CB GLN B 484 76.416 108.768 157.735 1.00 107.20 2785 CG GLN B 484 75.352 109.285 158.681 1.00 78.17 2786 CD GLN B 484 74.564 110.423 158.077 1.00 122.38 2787 OE1 GLN B 484 75.132 111.338 157.474 1.00 88.01 2788 NE2 GLN B 484 73.248 110.378 158.238 1.00 132.45 2789 C GLN B 484 76.177 106.385 158.392 1.00 52.68 2790 O GLN B 484 75.234 106.268 157.616 1.00 96.63 2791 N LEU B 485 76.386 105.553 159.408 1.00 54.65 2792 CA LEU B 485 75.529 104.401 159.636 1.00 61.68 2793 CB LEU B 485 75.859 103.754 160.976 1.00 56.33 2794 CG LEU B 485 77.220 103.068 161.101 1.00 54.48 2795 CD1 LEU B 485 77.171 102.084 162.246 1.00 62.35 2796 CD2 LEU B 485 77.554 102.325 159.813 1.00 115.96 2797 C LEU B 485 74.025 104.629 159.534 1.00 77.38 2798 O LEU B 485 73.537 105.746 159.679 1.00 81.23 2799 N PRO B 486 73.271 103.551 159.266 1.00 73.49 2800 CD PRO B 486 73.794 102.217 158.934 1.00 122.28 2801 CA PRO B 486 71.819 103.570 159.127 1.00 82.90 2802 CB PRO B 486 71.492 102.137 158.712 1.00 119.65 2803 CG PRO B 486 72.729 101.692 158.018 1.00 136.98 2804 C PRO B 486 71.154 103.952 160.433 1.00 94.37 2805 O PRO B 486 71.429 103.370 161.481 1.00 68.92 2806 N ASP B 487 70.268 104.932 160.359 1.00 84.31 2807 CA ASP B 487 69.560 105.398 161.533 1.00 88.88 2808 CB ASP B 487 68.424 106.329 161.097 1.00 108.41 2809 CG ASP B 487 68.070 107.347 162.155 1.00 154.62 2810 OD1 ASP B 487 67.549 106.946 163.217 1.00 160.64 2811 OD2 ASP B 487 68.322 108.549 161.926 1.00 168.53 2812 C ASP B 487 69.014 104.240 162.374 1.00 63.64 2813 O ASP B 487 69.085 104.269 163.596 1.00 90.99 2814 N ALA B 488 68.492 103.210 161.721 1.00 64.28 2815 CA ALA B 488 67.910 102.073 162.432 1.00 73.64 2816 CB ALA B 488 67.073 101.232 161.463 1.00 116.29 2817 C ALA B 488 68.921 101.189 163.143 1.00 75.09 2818 O ALA B 488 68.563 100.164 163.722 1.00 61.17 2819 N ARG B 489 70.180 101.599 163.122 1.00 47.46 2820 CA ARG B 489 71.245 100.817 163.739 1.00 76.59 2821 CB ARG B 489 72.562 101.088 163.014 1.00 92.18 2822 CG ARG B 489 72.771 100.227 161.785 1.00 116.98 2823 CD ARG B 489 73.469 98.935 162.162 1.00 101.72 2824 NE ARG B 489 74.904 99.013 161.904 1.00 96.78 2825 CZ ARG B 489 75.803 98.212 162.459 1.00 108.26 2826 NH1 ARG B 489 75.418 97.273 163.311 1.00 104.09 2827 NH2 ARG B 489 77.084 98.345 162.157 1.00 106.78 2828 C ARG B 489 71.432 101.066 165.219 1.00 78.64 2829 O ARG B 489 71.773 100.153 165.972 1.00 80.15 2830 N HIS B 490 71.205 102.308 165.631 1.00 85.57 2831 CA HIS B 490 71.377 102.703 167.023 1.00 79.08 2832 CB HIS B 490 72.359 103.863 167.106 1.00 65.14 2833 CG HIS B 490 71.883 105.094 166.405 1.00 51.35 2834 CD2 HIS B 490 70.847 105.924 166.669 1.00 81.18 2835 ND1 HIS B 490 72.493 105.592 165.276 1.00 77.41 2836 CE1 HIS B 490 71.855 106.678 164.874 1.00 76.90 2837 NE2 HIS B 490 70.852 106.901 165.703 1.00 118.70 2838 C HIS B 490 70.086 103.134 167.690 1.00 75.63 2839 O HIS B 490 69.136 103.545 167.028 1.00 82.18 2840 N SER B 491 70.072 103.056 169.017 1.00 111.19 2841 CA SER B 491 68.915 103.461 169.801 1.00 98.54 2842 CB SER B 491 68.477 102.333 170.737 1.00 70.59 2843 OG SER B 491 67.305 102.703 171.444 1.00 151.07 2844 C SER B 491 69.295 104.683 170.624 1.00 91.58 2845 O SER B 491 70.209 104.630 171.439 1.00 69.75 2846 N THR B 492 68.600 105.790 170.402 1.00 103.48 2847 CA THR B 492 68.874 107.011 171.149 1.00 84.76 2848 CB THR B 492 69.182 108.171 170.208 1.00 96.92 2849 OG1 THR B 492 70.431 107.927 169.553 1.00 98.55 2850 CG2 THR B 492 69.260 109.473 170.978 1.00 89.03 2851 C THR B 492 67.666 107.370 172.002 1.00 95.54 2852 O THR B 492 66.532 107.352 171.523 1.00 110.69 2853 N THR B 493 67.907 107.702 173.266 1.00 65.05 2854 CA THR B 493 66.809 108.036 174.159 1.00 70.59 2855 CB THR B 493 67.188 107.882 175.635 1.00 74.90 2856 OG1 THR B 493 68.008 108.984 176.019 1.00 55.82 2857 CG2 THR B 493 67.929 106.576 175.874 1.00 80.05 2858 C THR B 493 66.315 109.457 173.978 1.00 81.61 2859 O THR B 493 66.765 110.190 173.102 1.00 64.79 2860 N GLN B 494 65.365 109.834 174.820 1.00 97.42 2861 CA GLN B 494 64.806 111.166 174.769 1.00 90.31 2862 CB GLN B 494 63.296 111.115 175.033 1.00 108.14 2863 CG GLN B 494 62.486 110.334 174.005 1.00 116.36 2864 CD GLN B 494 62.660 110.860 172.584 1.00 154.38 2865 OE1 GLN B 494 62.652 112.070 172.350 1.00 129.72 2866 NE2 GLN B 494 62.804 109.947 171.627 1.00 166.89 2867 C GLN B 494 65.498 112.012 175.833 1.00 107.40 2868 O GLN B 494 65.869 111.509 176.900 1.00 110.85 2869 N PRO B 495 65.697 113.309 175.547 1.00 81.82 2870 CD PRO B 495 65.416 113.972 174.261 1.00 69.03 2871 CA PRO B 495 66.342 114.240 176.470 1.00 65.90 2872 CB PRO B 495 66.109 115.583 175.802 1.00 63.09 2873 CG PRO B 495 66.235 115.239 174.363 1.00 52.88 2874 C PRO B 495 65.742 114.186 177.867 1.00 75.89 2875 O PRO B 495 64.558 113.914 178.039 1.00 107.23 2876 N ARG B 496 66.580 114.437 178.862 1.00 112.34 2877 CA ARG B 496 66.166 114.445 180.257 1.00 123.31 2878 CB ARG B 496 66.434 113.080 180.902 1.00 145.69 2879 CG ARG B 496 65.366 112.031 180.599 1.00 159.05 2880 CD ARG B 496 65.774 110.643 181.091 1.00 178.53 2881 NE ARG B 496 64.643 109.715 181.137 1.00 209.19 2882 CZ ARG B 496 63.715 109.707 182.092 1.00 207.25 2883 NH1 ARG B 496 63.779 110.578 183.092 1.00 201.73 2884 NH2 ARG B 496 62.717 108.832 182.044 1.00 194.79 2885 C ARG B 496 66.963 115.549 180.944 1.00 134.53 2886 O ARG B 496 68.121 115.798 180.597 1.00 112.03 2887 N LYS B 497 66.341 116.220 181.907 1.00 136.67 2888 CA LYS B 497 66.999 117.318 182.601 1.00 99.35 2889 CB LYS B 497 65.955 118.224 183.252 1.00 115.41 2890 CG LYS B 497 64.939 118.793 182.278 1.00 150.70 2891 CD LYS B 497 63.952 119.718 182.976 1.00 164.39 2892 CE LYS B 497 62.907 120.251 182.003 1.00 162.23 2893 NZ LYS B 497 61.957 121.204 182.648 1.00 146.92 2894 C LYS B 497 68.005 116.876 183.649 1.00 102.60 2895 O LYS B 497 67.966 115.743 184.129 1.00 95.44 2896 N THR B 498 68.906 117.792 183.993 1.00 121.19 2897 CA THR B 498 69.940 117.543 184.989 1.00 137.86 2898 CB THR B 498 71.330 117.388 184.326 1.00 127.01 2899 OG1 THR B 498 71.571 118.479 183.426 1.00 102.85 2900 CG2 THR B 498 71.398 116.094 183.555 1.00 140.90 2901 C THR B 498 69.995 118.681 186.008 1.00 162.55 2902 O THR B 498 69.507 119.788 185.754 1.00 135.49 2903 N LYS B 499 70.589 118.405 187.164 1.00 151.73 2904 CA LYS B 499 70.701 119.410 188.212 1.00 168.61 2905 CB LYS B 499 71.167 118.755 189.520 1.00 183.90 2906 CG LYS B 499 70.993 119.632 190.759 1.00 193.98 2907 CD LYS B 499 71.224 118.849 192.051 1.00 178.03 2908 CE LYS B 499 70.926 119.704 193.283 1.00 168.01 2909 NZ LYS B 499 71.031 118.937 194.562 1.00 137.47 2910 C LYS B 499 71.677 120.509 187.780 1.00 173.90 2911 O LYS B 499 72.200 121.257 188.606 1.00 189.46 2912 N GLY B 500 71.910 120.597 186.473 1.00 172.18 2913 CA GLY B 500 72.811 121.601 185.936 1.00 169.02 2914 C GLY B 500 72.141 122.406 184.837 1.00 176.17 2915 O GLY B 500 72.813 122.959 183.965 1.00 182.74 2916 N SER B 501 70.810 122.456 184.884 1.00 151.02 2917 CA SER B 501 69.989 123.189 183.919 1.00 147.04 2918 CB SER B 501 70.242 124.698 184.044 1.00 152.23 2919 OG SER B 501 71.556 125.048 183.642 1.00 182.63 2920 C SER B 501 70.164 122.762 182.458 1.00 151.49 2921 O SER B 501 69.620 123.395 181.549 1.00 133.52 2922 N GLY B 502 70.916 121.691 182.230 1.00 142.82 2923 CA GLY B 502 71.116 121.218 180.873 1.00 95.52 2924 C GLY B 502 70.507 119.842 180.705 1.00 118.00 2925 O GLY B 502 70.114 119.219 181.689 1.00 106.89 2926 N PHE B 503 70.421 119.358 179.469 1.00 108.44 2927 CA PHE B 503 69.850 118.035 179.231 1.00 93.09 2928 CB PHE B 503 68.868 118.051 178.071 1.00 70.27 2929 CG PHE B 503 67.813 119.092 178.173 1.00 78.42 2930 CD1 PHE B 503 68.002 120.346 177.604 1.00 94.67 2931 CD2 PHE B 503 66.605 118.803 178.782 1.00 58.13 2932 CE1 PHE B 503 66.990 121.300 177.635 1.00 98.84 2933 CE2 PHE B 503 65.587 119.749 178.819 1.00 113.56 2934 CZ PHE B 503 65.779 121.001 178.243 1.00 112.26 2935 C PHE B 503 70.909 116.995 178.911 1.00 91.24 2936 O PHE B 503 72.074 117.326 178.682 1.00 63.55 2937 N PHE B 504 70.474 115.737 178.867 1.00 71.28 2938 CA PHE B 504 71.354 114.618 178.578 1.00 66.45 2939 CB PHE B 504 71.965 114.102 179.879 1.00 66.76 2940 CG PHE B 504 71.102 113.121 180.617 1.00 55.05 2941 CD1 PHE B 504 71.121 111.776 180.286 1.00 75.50 2942 CD2 PHE B 504 70.308 113.532 181.672 1.00 92.55 2943 CE1 PHE B 504 70.367 110.853 181.003 1.00 87.60 2944 CE2 PHE B 504 69.551 112.614 182.394 1.00 119.03 2945 CZ PHE B 504 69.583 111.271 182.057 1.00 113.46 2946 C PHE B 504 70.627 113.477 177.864 1.00 71.40 2947 O PHE B 504 69.534 113.078 178.262 1.00 98.42 2948 N VAL B 505 71.240 112.949 176.809 1.00 93.14 2949 CA VAL B 505 70.652 111.844 176.061 1.00 85.70 2950 CB VAL B 505 70.169 112.299 174.672 1.00 64.09 2951 CG1 VAL B 505 71.345 112.676 173.807 1.00 32.54 2952 CG2 VAL B 505 69.357 111.195 174.029 1.00 103.96 2953 C VAL B 505 71.669 110.722 175.888 1.00 58.13 2954 O VAL B 505 72.859 110.973 175.798 1.00 86.55 2955 N PHE B 506 71.187 109.487 175.841 1.00 81.98 2956 CA PHE B 506 72.035 108.311 175.685 1.00 63.87 2957 CB PHE B 506 71.733 107.331 176.792 1.00 50.64 2958 CG PHE B 506 72.585 107.497 178.006 1.00 61.69 2959 CD1 PHE B 506 72.100 107.129 179.255 1.00 87.69 2960 CD2 PHE B 506 73.900 107.921 177.902 1.00 101.17 2961 CE1 PHE B 506 72.904 107.168 180.385 1.00 55.65 2962 CE2 PHE B 506 74.721 107.965 179.032 1.00 102.15 2963 CZ PHE B 506 74.218 107.584 180.275 1.00 83.88 2964 C PHE B 506 71.816 107.605 174.357 1.00 71.24 2965 O PHE B 506 70.699 107.567 173.845 1.00 133.97 2966 N SER B 507 72.883 107.036 173.803 1.00 84.07 2967 CA SER B 507 72.801 106.312 172.533 1.00 76.16 2968 CB SER B 507 73.454 107.090 171.405 1.00 27.10 2969 OG SER B 507 73.355 106.340 170.220 1.00 58.51 2970 C SER B 507 73.480 104.962 172.635 1.00 57.27 2971 O SER B 507 74.493 104.821 173.310 1.00 52.02 2972 N ARG B 508 72.924 103.967 171.958 1.00 51.27 2973 CA ARG B 508 73.476 102.616 172.002 1.00 53.55 2974 CB ARG B 508 72.623 101.735 172.911 1.00 44.14 2975 CG ARG B 508 72.985 100.277 172.923 1.00 46.22 2976 CD ARG B 508 72.144 99.540 173.949 1.00 70.79 2977 NE ARG B 508 72.340 98.093 173.925 1.00 49.24 2978 CZ ARG B 508 71.855 97.291 172.984 1.00 103.44 2979 NH1 ARG B 508 71.147 97.796 171.984 1.00 133.71 2980 NH2 ARG B 508 72.064 95.983 173.054 1.00 124.77 2981 C ARG B 508 73.541 102.032 170.601 1.00 62.86 2982 O ARG B 508 72.555 102.020 169.864 1.00 86.63 2983 N LEU B 509 74.718 101.531 170.248 1.00 101.57 2984 CA LEU B 509 74.962 100.979 168.925 1.00 91.96 2985 CB LEU B 509 75.820 101.966 168.140 1.00 57.86 2986 CG LEU B 509 76.358 101.480 166.804 1.00 69.57 2987 CD1 LEU B 509 75.215 100.940 165.972 1.00 115.82 2988 CD2 LEU B 509 77.045 102.618 166.093 1.00 47.22 2989 C LEU B 509 75.656 99.623 168.930 1.00 72.22 2990 O LEU B 509 76.871 99.577 168.926 1.00 65.45 2991 N GLU B 510 74.902 98.526 168.928 1.00 103.54 2992 CA GLU B 510 75.513 97.191 168.921 1.00 79.97 2993 CB GLU B 510 74.427 96.107 168.847 1.00 105.98 2994 CG GLU B 510 73.491 96.056 170.061 1.00 124.66 2995 CD GLU B 510 72.349 95.050 169.905 1.00 156.13 2996 OE1 GLU B 510 71.488 95.247 169.018 1.00 161.88 2997 OE2 GLU B 510 72.309 94.061 170.673 1.00 131.37 2998 C GLU B 510 76.445 97.095 167.708 1.00 100.86 2999 O GLU B 510 76.171 97.705 166.671 1.00 97.53 3000 N VAL B 511 77.540 96.339 167.834 1.00 86.41 3001 CA VAL B 511 78.512 96.196 166.741 1.00 113.22 3002 CB VAL B 511 79.763 97.091 166.993 1.00 29.35 3003 CG1 VAL B 511 80.823 96.827 165.953 1.00 119.74 3004 CG2 VAL B 511 79.373 98.544 166.915 1.00 108.86 3005 C VAL B 511 78.981 94.760 166.461 1.00 152.83 3006 O VAL B 511 78.941 93.899 167.343 1.00 151.08 3007 N THR B 512 79.428 94.522 165.225 1.00 167.98 3008 CA THR B 512 79.908 93.212 164.786 1.00 153.93 3009 CB THR B 512 79.252 92.806 163.446 1.00 164.28 3010 OG1 THR B 512 77.826 92.831 163.583 1.00 167.99 3011 CG2 THR B 512 79.691 91.403 163.034 1.00 183.03 3012 C THR B 512 81.427 93.180 164.604 1.00 134.07 3013 O THR B 512 82.018 94.132 164.093 1.00 85.13 3014 N ARG B 513 82.042 92.071 165.017 1.00 128.25 3015 CA ARG B 513 83.488 91.879 164.910 1.00 132.09 3016 CB ARG B 513 83.853 90.401 165.116 1.00 158.22 3017 CG ARG B 513 85.357 90.120 165.061 1.00 185.92 3018 CD ARG B 513 85.684 88.632 165.174 1.00 210.68 3019 NE ARG B 513 87.125 88.379 165.106 1.00 235.05 3020 CZ ARG B 513 87.683 87.170 165.129 1.00 237.14 3021 NH1 ARG B 513 86.926 86.085 165.219 1.00 231.50 3022 NH2 ARG B 513 89.003 87.045 165.060 1.00 226.13 3023 C ARG B 513 84.028 92.345 163.566 1.00 119.35 3024 O ARG B 513 84.945 93.157 163.504 1.00 73.78 3025 N ALA B 514 83.450 91.824 162.492 1.00 114.41 3026 CA ALA B 514 83.868 92.174 161.147 1.00 105.99 3027 CB ALA B 514 82.798 91.766 160.171 1.00 110.57 3028 C ALA B 514 84.167 93.657 160.992 1.00 106.98 3029 O ALA B 514 85.169 94.038 160.389 1.00 114.61 3030 N GLU B 515 83.303 94.493 161.550 1.00 107.80 3031 CA GLU B 515 83.461 95.936 161.440 1.00 100.76 3032 CB GLU B 515 82.162 96.623 161.855 1.00 61.09 3033 CG GLU B 515 81.038 96.378 160.880 1.00 142.67 3034 CD GLU B 515 79.733 96.989 161.327 1.00 158.22 3035 OE1 GLU B 515 79.234 96.590 162.401 1.00 121.42 3036 OE2 GLU B 515 79.210 97.862 160.600 1.00 163.79 3037 C GLU B 515 84.637 96.589 162.164 1.00 105.34 3038 O GLU B 515 85.189 97.567 161.664 1.00 78.08 3039 N TRP B 516 85.034 96.082 163.327 1.00 77.37 3040 CA TRP B 516 86.146 96.723 164.007 1.00 80.12 3041 CB TRP B 516 86.035 96.570 165.523 1.00 104.80 3042 CG TRP B 516 86.442 95.275 166.113 1.00 71.05 3043 CD2 TRP B 516 85.591 94.349 166.786 1.00 78.16 3044 CE2 TRP B 516 86.411 93.335 167.314 1.00 93.47 3045 CE3 TRP B 516 84.211 94.281 166.999 1.00 89.55 3046 CD1 TRP B 516 87.708 94.795 166.243 1.00 118.89 3047 NE1 TRP B 516 87.702 93.630 166.968 1.00 138.68 3048 CZ2 TRP B 516 85.896 92.262 168.043 1.00 130.46 3049 CZ3 TRP B 516 83.698 93.218 167.722 1.00 72.54 3050 CH2 TRP B 516 84.539 92.222 168.236 1.00 115.85 3051 C TRP B 516 87.493 96.250 163.505 1.00 126.19 3052 O TRP B 516 88.524 96.836 163.833 1.00 155.29 3053 N GLU B 517 87.484 95.191 162.703 1.00 127.20 3054 CA GLU B 517 88.715 94.681 162.120 1.00 102.94 3055 CB GLU B 517 88.586 93.193 161.804 1.00 124.17 3056 CG GLU B 517 88.437 92.331 163.045 1.00 150.03 3057 CD GLU B 517 88.603 90.854 162.756 1.00 194.54 3058 OE1 GLU B 517 87.847 90.322 161.915 1.00 209.80 3059 OE2 GLU B 517 89.490 90.226 163.373 1.00 178.99 3060 C GLU B 517 88.923 95.495 160.848 1.00 118.06 3061 O GLU B 517 90.047 95.697 160.396 1.00 141.82 3062 N GLN B 518 87.817 95.976 160.289 1.00 96.99 3063 CA GLN B 518 87.840 96.803 159.093 1.00 108.10 3064 CB GLN B 518 86.407 97.051 158.611 1.00 144.13 3065 CG GLN B 518 86.285 97.795 157.287 1.00 173.67 3066 CD GLN B 518 84.834 98.105 156.921 1.00 166.01 3067 OE1 GLN B 518 83.989 97.206 156.851 1.00 119.41 3068 NE2 GLN B 518 84.544 99.382 156.686 1.00 143.37 3069 C GLN B 518 88.500 98.116 159.504 1.00 120.74 3070 O GLN B 518 89.196 98.743 158.710 1.00 92.65 3071 N LYS B 519 88.260 98.509 160.758 1.00 130.00 3072 CA LYS B 519 88.818 99.719 161.375 1.00 130.50 3073 CB LYS B 519 88.367 100.990 160.643 1.00 69.93 3074 CG LYS B 519 89.179 102.223 161.053 1.00 87.64 3075 CD LYS B 519 89.180 103.305 159.981 1.00 120.11 3076 CE LYS B 519 90.255 104.358 160.255 1.00 120.69 3077 NZ LYS B 519 90.332 105.388 159.175 1.00 139.23 3078 C LYS B 519 88.370 99.789 162.835 1.00 113.46 3079 O LYS B 519 87.399 99.145 163.209 1.00 100.53 3080 N ASP B 520 89.086 100.555 163.656 1.00 141.80 3081 CA ASP B 520 88.752 100.712 165.075 1.00 91.69 3082 CB ASP B 520 90.013 100.687 165.939 1.00 139.47 3083 CG ASP B 520 90.474 99.285 166.259 1.00 176.31 3084 OD1 ASP B 520 89.710 98.566 166.935 1.00 155.37 3085 OD2 ASP B 520 91.593 98.907 165.843 1.00 179.10 3086 C ASP B 520 88.026 102.029 165.323 1.00 88.08 3087 O ASP B 520 87.179 102.115 166.201 1.00 108.19 3088 N GLU B 521 88.367 103.055 164.552 1.00 111.16 3089 CA GLU B 521 87.745 104.369 164.690 1.00 96.48 3090 CB GLU B 521 88.335 105.364 163.686 1.00 137.30 3091 CG GLU B 521 89.404 106.294 164.229 1.00 154.75 3092 CD GLU B 521 89.685 107.446 163.278 1.00 162.73 3093 OE1 GLU B 521 88.761 108.254 163.051 1.00 123.78 3094 OE2 GLU B 521 90.818 107.542 162.754 1.00 170.68 3095 C GLU B 521 86.236 104.373 164.495 1.00 94.12 3096 O GLU B 521 85.750 104.213 163.377 1.00 98.75 3097 N PHE B 522 85.506 104.574 165.588 1.00 125.98 3098 CA PHE B 522 84.052 104.669 165.563 1.00 73.40 3099 CB PHE B 522 83.424 103.654 166.495 1.00 46.93 3100 CG PHE B 522 83.252 102.307 165.892 1.00 88.24 3101 CD1 PHE B 522 84.291 101.701 165.210 1.00 107.06 3102 CD2 PHE B 522 82.051 101.625 166.026 1.00 126.15 3103 CE1 PHE B 522 84.137 100.430 164.671 1.00 144.12 3104 CE2 PHE B 522 81.887 100.353 165.491 1.00 86.55 3105 CZ PHE B 522 82.929 99.756 164.814 1.00 98.88 3106 C PHE B 522 83.737 106.065 166.062 1.00 85.06 3107 O PHE B 522 84.219 106.486 167.113 1.00 76.66 3108 N ILE B 523 82.937 106.797 165.313 1.00 64.62 3109 CA ILE B 523 82.619 108.140 165.731 1.00 93.86 3110 CB ILE B 523 83.006 109.136 164.638 1.00 62.16 3111 CG2 ILE B 523 82.726 110.554 165.093 1.00 77.13 3112 CG1 ILE B 523 84.483 108.963 164.309 1.00 68.68 3113 CD1 ILE B 523 85.004 109.946 163.268 1.00 144.70 3114 C ILE B 523 81.152 108.304 166.076 1.00 89.50 3115 O ILE B 523 80.276 107.800 165.371 1.00 97.40 3116 N CYS B 524 80.903 108.998 167.183 1.00 89.54 3117 CA CYS B 524 79.551 109.286 167.642 1.00 88.30 3118 C CYS B 524 79.358 110.792 167.558 1.00 53.16 3119 O CYS B 524 79.589 111.496 168.514 1.00 59.51 3120 CB CYS B 524 79.363 108.835 169.082 1.00 70.18 3121 SG CYS B 524 77.896 109.575 169.868 1.00 102.40 3122 N ARG B 525 78.939 111.272 166.397 1.00 85.33 3123 CA ARG B 525 78.740 112.694 166.166 1.00 42.18 3124 CB ARG B 525 78.613 112.956 164.664 1.00 51.31 3125 CG ARG B 525 78.750 114.395 164.270 1.00 55.59 3126 CD ARG B 525 79.294 114.553 162.852 1.00 75.11 3127 NE ARG B 525 78.328 114.264 161.795 1.00 77.64 3128 CZ ARG B 525 78.518 114.587 160.517 1.00 147.54 3129 NH1 ARG B 525 79.633 115.211 160.143 1.00 139.91 3130 NH2 ARG B 525 77.598 114.280 159.610 1.00 128.34 3131 C ARG B 525 77.501 113.197 166.880 1.00 81.14 3132 O ARG B 525 76.714 112.411 167.406 1.00 77.17 3133 N ALA B 526 77.344 114.517 166.897 1.00 86.44 3134 CA ALA B 526 76.209 115.177 167.538 1.00 64.44 3135 CB ALA B 526 76.469 115.358 169.025 1.00 40.12 3136 C ALA B 526 76.003 116.527 166.881 1.00 64.81 3137 O ALA B 526 76.957 117.256 166.609 1.00 75.52 3138 N VAL B 527 74.753 116.858 166.616 1.00 45.76 3139 CA VAL B 527 74.446 118.123 165.984 1.00 48.87 3140 CB VAL B 527 73.702 117.900 164.683 1.00 72.30 3141 CG1 VAL B 527 73.434 119.222 164.005 1.00 65.22 3142 CG2 VAL B 527 74.512 116.984 163.798 1.00 69.67 3143 C VAL B 527 73.583 118.949 166.912 1.00 62.63 3144 O VAL B 527 72.494 118.525 167.296 1.00 107.55 3145 N HIS B 528 74.075 120.123 167.290 1.00 88.39 3146 CA HIS B 528 73.324 121.009 168.177 1.00 72.81 3147 CB HIS B 528 73.883 120.954 169.599 1.00 43.78 3148 CG HIS B 528 73.000 121.603 170.619 1.00 68.69 3149 CD2 HIS B 528 72.544 122.873 170.730 1.00 102.41 3150 ND1 HIS B 528 72.530 120.932 171.727 1.00 114.24 3151 CE1 HIS B 528 71.828 121.761 172.479 1.00 111.59 3152 NE2 HIS B 528 71.822 122.946 171.896 1.00 127.17 3153 C HIS B 528 73.405 122.421 167.644 1.00 69.99 3154 O HIS B 528 74.322 122.745 166.877 1.00 80.61 3155 N GLU B 529 72.439 123.246 168.040 1.00 80.81 3156 CA GLU B 529 72.388 124.630 167.603 1.00 110.94 3157 CB GLU B 529 71.056 125.236 168.007 1.00 143.10 3158 CG GLU B 529 70.885 126.632 167.550 1.00 190.23 3159 CD GLU B 529 69.576 127.233 168.045 1.00 209.79 3160 OE1 GLU B 529 69.275 128.356 168.100 1.00 211.79 3161 OE2 GLU B 529 68.633 126.689 168.465 1.00 204.23 3162 C GLU B 529 73.552 125.453 168.173 1.00 115.08 3163 O GLU B 529 73.915 126.492 167.625 1.00 93.09 3164 N ALA B 530 74.184 124.942 169.228 1.00 104.56 3165 CA ALA B 530 75.301 125.633 169.882 1.00 119.10 3166 CB ALA B 530 75.312 125.312 171.383 1.00 102.81 3167 C ALA B 530 76.657 125.298 169.285 1.00 143.44 3168 O ALA B 530 77.105 125.948 168.341 1.00 167.11 3169 N ALA B 531 77.296 124.287 169.868 1.00 133.04 3170 CA ALA B 531 78.608 123.796 169.457 1.00 161.80 3171 CB ALA B 531 78.530 122.299 169.233 1.00 131.50 3172 C ALA B 531 79.240 124.461 168.235 1.00 183.35 3173 O ALA B 531 78.602 124.634 167.193 1.00 180.45 3174 N SER B 532 80.513 124.816 168.369 1.00 186.13 3175 CA SER B 532 81.245 125.437 167.279 1.00 159.85 3176 CB SER B 532 81.945 126.707 167.764 1.00 149.12 3177 OG SER B 532 81.012 127.751 167.971 1.00 131.01 3178 C SER B 532 82.270 124.459 166.721 1.00 143.48 3179 O SER B 532 82.606 123.460 167.359 1.00 131.10 3180 N PRO B 533 82.789 124.741 165.522 1.00 133.12 3181 CD PRO B 533 84.018 124.105 165.014 1.00 145.42 3182 CA PRO B 533 82.446 125.915 164.718 1.00 114.44 3183 CB PRO B 533 83.793 126.336 164.170 1.00 151.25 3184 CG PRO B 533 84.400 124.997 163.830 1.00 156.89 3185 C PRO B 533 81.477 125.558 163.605 1.00 132.46 3186 O PRO B 533 80.902 126.440 162.963 1.00 100.35 3187 N SER B 534 81.320 124.256 163.383 1.00 143.66 3188 CA SER B 534 80.452 123.734 162.335 1.00 132.97 3189 CB SER B 534 81.191 122.649 161.552 1.00 161.58 3190 OG SER B 534 81.699 121.659 162.433 1.00 165.58 3191 C SER B 534 79.150 123.167 162.880 1.00 119.62 3192 O SER B 534 78.478 122.386 162.208 1.00 111.21 3193 N GLN B 535 78.797 123.562 164.097 1.00 121.56 3194 CA GLN B 535 77.567 123.100 164.729 1.00 104.19 3195 CB GLN B 535 76.364 123.514 163.874 1.00 39.24 3196 CG GLN B 535 76.251 125.023 163.741 1.00 73.06 3197 CD GLN B 535 76.192 125.485 162.297 1.00 105.92 3198 OE1 GLN B 535 76.935 124.993 161.445 1.00 122.35 3199 NE2 GLN B 535 75.317 126.449 162.017 1.00 116.95 3200 C GLN B 535 77.588 121.590 164.945 1.00 81.66 3201 O GLN B 535 76.565 120.977 165.244 1.00 75.14 3202 N THR B 536 78.772 121.005 164.809 1.00 75.59 3203 CA THR B 536 78.960 119.571 164.983 1.00 73.02 3204 CB THR B 536 79.677 118.967 163.771 1.00 96.53 3205 OG1 THR B 536 78.861 119.117 162.604 1.00 138.70 3206 CG2 THR B 536 79.973 117.509 164.005 1.00 87.18 3207 C THR B 536 79.825 119.321 166.200 1.00 72.59 3208 O THR B 536 80.514 120.215 166.672 1.00 108.65 3209 N VAL B 537 79.798 118.095 166.694 1.00 58.96 3210 CA VAL B 537 80.600 117.708 167.847 1.00 83.66 3211 CB VAL B 537 79.969 118.190 169.146 1.00 52.09 3212 CG1 VAL B 537 80.474 117.351 170.311 1.00 68.77 3213 CG2 VAL B 537 80.317 119.645 169.366 1.00 119.61 3214 C VAL B 537 80.723 116.195 167.904 1.00 99.63 3215 O VAL B 537 79.719 115.495 167.960 1.00 109.69 3216 N GLN B 538 81.947 115.685 167.904 1.00 100.40 3217 CA GLN B 538 82.128 114.242 167.931 1.00 90.82 3218 CB GLN B 538 82.389 113.741 166.508 1.00 92.68 3219 CG GLN B 538 83.519 114.462 165.790 1.00 69.71 3220 CD GLN B 538 83.524 114.199 164.292 1.00 97.76 3221 OE1 GLN B 538 82.734 114.776 163.543 1.00 78.04 3222 NE2 GLN B 538 84.410 113.314 163.850 1.00 116.83 3223 C GLN B 538 83.238 113.781 168.859 1.00 75.38 3224 O GLN B 538 84.090 114.568 169.262 1.00 96.22 3225 N ARG B 539 83.206 112.500 169.206 1.00 51.75 3226 CA ARG B 539 84.215 111.907 170.074 1.00 99.09 3227 CB ARG B 539 83.719 111.803 171.517 1.00 100.20 3228 CG ARG B 539 84.820 111.481 172.533 1.00 145.36 3229 CD ARG B 539 85.250 112.726 173.313 1.00 159.80 3230 NE ARG B 539 85.363 113.903 172.451 1.00 167.91 3231 CZ ARG B 539 85.663 115.127 172.880 1.00 150.28 3232 NH1 ARG B 539 85.887 115.344 174.170 1.00 164.72 3233 NH2 ARG B 539 85.726 116.136 172.017 1.00 114.07 3234 C ARG B 539 84.493 110.512 169.547 1.00 119.86 3235 O ARG B 539 83.580 109.700 169.426 1.00 90.13 3236 N ALA B 540 85.753 110.236 169.234 1.00 128.12 3237 CA ALA B 540 86.136 108.933 168.712 1.00 89.16 3238 CB ALA B 540 87.531 109.015 168.111 1.00 124.98 3239 C ALA B 540 86.100 107.866 169.796 1.00 76.22 3240 O ALA B 540 86.009 108.171 170.980 1.00 109.84 3241 N VAL B 541 86.173 106.612 169.376 1.00 60.52 3242 CA VAL B 541 86.179 105.491 170.303 1.00 86.69 3243 CB VAL B 541 84.770 105.139 170.724 1.00 87.58 3244 CG1 VAL B 541 84.005 104.682 169.512 1.00 77.89 3245 CG2 VAL B 541 84.785 104.059 171.807 1.00 52.44 3246 C VAL B 541 86.786 104.283 169.597 1.00 102.20 3247 O VAL B 541 87.163 104.375 168.430 1.00 152.01 3248 N SER B 542 86.882 103.159 170.306 1.00 105.84 3249 CA SER B 542 87.426 101.922 169.748 1.00 89.13 3250 CB SER B 542 88.722 102.199 168.975 1.00 113.60 3251 OG SER B 542 89.682 102.852 169.791 1.00 119.14 3252 C SER B 542 87.713 100.893 170.829 1.00 69.68 3253 O SER B 542 87.935 101.248 171.987 1.00 134.26 3254 N VAL B 543 87.710 99.618 170.452 1.00 64.03 3255 CA VAL B 543 88.017 98.550 171.401 1.00 113.44 3256 CB VAL B 543 87.339 97.221 171.023 1.00 126.85 3257 CG1 VAL B 543 87.101 96.404 172.285 1.00 62.70 3258 CG2 VAL B 543 86.055 97.470 170.223 1.00 22.03 3259 C VAL B 543 89.530 98.308 171.372 1.00 152.87 3260 O VAL B 543 90.183 98.571 170.361 1.00 170.87 3261 N ASN B 544 90.079 97.799 172.472 1.00 147.76 3262 CA ASN B 544 91.511 97.522 172.561 1.00 158.75 3263 CB ASN B 544 91.944 96.576 171.431 1.00 162.14 3264 CG ASN B 544 91.163 95.267 171.423 1.00 149.81 3265 OD1 ASN B 544 91.128 94.541 172.417 1.00 152.63 3266 ND2 ASN B 544 90.540 94.958 170.289 1.00 96.95 3267 C ASN B 544 92.336 98.814 172.498 1.00 165.23 3268 O ASN B 544 93.135 99.041 173.435 1.00 169.09 3269 OXT ASN B 544 92.179 99.582 171.517 1.00 91.11 3270 C1 NAG B 694 43.351 106.499 163.692 1.00 45.89 3271 C2 NAG B 694 43.324 107.210 165.050 1.00 60.23 3272 N2 NAG B 694 42.009 107.764 165.311 1.00 56.36 3273 C7 NAG B 694 41.107 107.072 166.005 1.00 75.39 3274 O7 NAG B 694 41.224 105.878 166.283 1.00 71.41 3275 C8 NAG B 694 39.876 107.819 166.449 1.00 22.03 3276 C3 NAG B 694 44.367 108.326 165.119 1.00 58.80 3277 O3 NAG B 694 44.468 108.774 166.459 1.00 74.72 3278 C4 NAG B 694 45.745 107.860 164.653 1.00 56.10 3279 O4 NAG B 694 46.595 109.009 164.472 1.00 83.05 3280 C5 NAG B 694 45.633 107.121 163.324 1.00 25.95 3281 O5 NAG B 694 44.683 106.052 163.418 1.00 53.24 3282 C6 NAG B 694 46.944 106.492 162.896 1.00 119.03 3283 O6 NAG B 694 46.718 105.307 162.144 1.00 138.62 3284 C1 NAG B 695 47.667 109.149 165.334 1.00 105.64 3285 C2 NAG B 695 48.912 109.587 164.537 1.00 59.77 3286 N2 NAG B 695 49.357 108.488 163.700 1.00 93.15 3287 C7 NAG B 695 49.909 108.731 162.516 1.00 103.18 3288 O7 NAG B 695 51.131 108.754 162.340 1.00 136.64 3289 C8 NAG B 695 48.960 108.985 161.349 1.00 60.78 3290 C3 NAG B 695 50.062 110.046 165.456 1.00 79.33 3291 O3 NAG B 695 51.051 110.680 164.656 1.00 98.62 3292 C4 NAG B 695 49.530 111.028 166.523 1.00 100.15 3293 O4 NAG B 695 50.546 111.348 167.496 1.00 82.39 3294 C5 NAG B 695 48.357 110.377 167.236 1.00 125.01 3295 O5 NAG B 695 47.306 110.143 166.294 1.00 76.78 3296 C6 NAG B 695 47.797 111.249 168.331 1.00 149.78 3297 O6 NAG B 695 46.422 110.979 168.540 1.00 106.46 3298 C1 MAN B 696 51.371 112.429 167.246 1.00 73.26 3299 C2 MAN B 696 51.896 112.953 168.555 1.00 85.84 3300 O2 MAN B 696 52.572 111.906 169.203 1.00 84.25 3301 C3 MAN B 696 52.858 114.113 168.311 1.00 120.67 3302 O3 MAN B 696 53.494 114.526 169.543 1.00 161.15 3303 C4 MAN B 696 53.939 113.688 167.318 1.00 142.38 3304 O4 MAN B 696 54.644 114.828 166.907 1.00 158.25 3305 C5 MAN B 696 53.376 112.998 166.077 1.00 122.76 3306 O5 MAN B 696 52.478 111.940 166.480 1.00 129.27 3307 C6 MAN B 696 54.495 112.437 165.214 1.00 121.56 3308 O6 MAN B 696 54.271 111.063 164.855 1.00 154.87 3309 C1 MAN B 697 55.439 110.276 165.023 1.00 145.40 3310 C2 MAN B 697 56.117 110.375 166.417 1.00 145.77 3311 O2 MAN B 697 57.047 109.270 166.517 1.00 146.40 3312 C3 MAN B 697 56.937 111.658 166.557 1.00 141.88 3313 O3 MAN B 697 57.844 111.476 167.629 1.00 137.62 3314 C4 MAN B 697 57.782 111.951 165.323 1.00 141.83 3315 O4 MAN B 697 58.361 113.247 165.387 1.00 139.00 3316 C5 MAN B 697 57.018 111.797 164.042 1.00 143.82 3317 O5 MAN B 697 56.422 110.499 164.016 1.00 146.27 3318 C6 MAN B 697 57.919 111.862 162.860 1.00 148.17 3319 O6 MAN B 697 57.262 111.446 161.673 1.00 150.80 3320 C1 MAN B 698 52.693 115.215 170.457 1.00 166.73 3321 C2 MAN B 698 53.464 116.407 171.056 1.00 180.10 3322 O2 MAN B 698 52.557 117.261 171.748 1.00 145.07 3323 C3 MAN B 698 54.563 115.916 172.016 1.00 172.30 3324 O3 MAN B 698 55.188 117.024 172.657 1.00 137.27 3325 C4 MAN B 698 53.964 114.962 173.060 1.00 164.34 3326 O4 MAN B 698 54.992 114.436 173.885 1.00 140.37 3327 C5 MAN B 698 53.231 113.819 172.351 1.00 150.05 3328 O5 MAN B 698 52.208 114.363 171.491 1.00 142.54 3329 C6 MAN B 698 52.553 112.858 173.311 1.00 146.09 3330 O6 MAN B 698 51.158 112.769 173.056 1.00 158.71 3331 C1 MAN B 699 56.966 108.431 167.643 1.00 147.68 3332 C2 MAN B 699 58.038 108.848 168.676 1.00 149.11 3333 O2 MAN B 699 57.797 108.220 169.928 1.00 144.31 3334 C3 MAN B 699 59.464 108.512 168.172 1.00 149.80 3335 O3 MAN B 699 60.421 108.765 169.197 1.00 142.63 3336 C4 MAN B 699 59.578 107.043 167.743 1.00 151.96 3337 O4 MAN B 699 60.851 106.815 167.127 1.00 149.52 3338 C5 MAN B 699 58.427 106.645 166.780 1.00 152.87 3339 O5 MAN B 699 57.110 107.042 167.306 1.00 150.31 3340 C6 MAN B 699 58.378 105.138 166.486 1.00 152.00 3341 O6 MAN B 699 58.826 104.348 167.584 1.00 155.30 3342 C CYS D 329 40.977 121.748 178.634 1.00 210.29 3343 O CYS D 329 41.782 122.273 179.404 1.00 189.25 3344 CB CYS D 329 41.494 121.206 176.231 1.00 224.93 3345 SG CYS D 329 39.884 121.730 175.555 1.00 250.42 3346 N CYS D 329 40.558 119.454 177.703 1.00 206.24 3347 CA CYS D 329 41.438 120.654 177.662 1.00 208.57 3348 N ASP D 330 39.687 122.084 178.603 1.00 212.05 3349 CA ASP D 330 39.131 123.119 179.482 1.00 192.97 3350 CB ASP D 330 38.840 124.395 178.679 1.00 200.39 3351 CG ASP D 330 38.321 125.535 179.549 1.00 207.96 3352 OD1 ASP D 330 37.203 125.420 180.100 1.00 182.28 3353 OD2 ASP D 330 39.037 126.552 179.681 1.00 213.37 3354 C ASP D 330 37.854 122.657 180.187 1.00 188.18 3355 O ASP D 330 37.908 122.095 181.282 1.00 170.40 3356 N SER D 331 36.707 122.905 179.557 1.00 186.14 3357 CA SER D 331 35.419 122.512 180.123 1.00 155.83 3358 CB SER D 331 34.266 123.184 179.364 1.00 152.11 3359 OG SER D 331 34.055 122.582 178.092 1.00 95.70 3360 C SER D 331 35.242 120.995 180.068 1.00 163.80 3361 O SER D 331 34.998 120.366 181.098 1.00 161.57 3362 N ASN D 332 35.368 120.419 178.869 1.00 159.48 3363 CA ASN D 332 35.214 118.978 178.678 1.00 122.47 3364 CB ASN D 332 35.786 118.530 177.325 1.00 172.30 3365 CG ASN D 332 37.269 118.836 177.170 1.00 223.31 3366 OD1 ASN D 332 37.916 119.341 178.087 1.00 239.48 3367 ND2 ASN D 332 37.816 118.520 175.998 1.00 237.24 3368 C ASN D 332 35.874 118.205 179.816 1.00 105.80 3369 O ASN D 332 37.091 118.207 179.975 1.00 93.15 3370 N PRO D 333 35.064 117.539 180.644 1.00 64.26 3371 CD PRO D 333 33.600 117.604 180.724 1.00 41.20 3372 CA PRO D 333 35.595 116.778 181.771 1.00 41.52 3373 CB PRO D 333 34.363 116.548 182.633 1.00 35.93 3374 CG PRO D 333 33.402 117.622 182.204 1.00 77.83 3375 C PRO D 333 36.222 115.480 181.314 1.00 54.76 3376 O PRO D 333 35.858 114.951 180.272 1.00 34.59 3377 N ARG D 334 37.160 114.976 182.107 1.00 19.96 3378 CA ARG D 334 37.866 113.731 181.813 1.00 40.10 3379 CB ARG D 334 39.389 113.936 181.935 1.00 60.92 3380 CG ARG D 334 40.245 112.697 181.633 1.00 28.56 3381 CD ARG D 334 41.745 112.986 181.457 1.00 78.41 3382 NE ARG D 334 42.377 112.028 180.545 1.00 73.15 3383 CZ ARG D 334 42.757 112.326 179.306 1.00 100.07 3384 NH1 ARG D 334 42.575 113.553 178.841 1.00 59.54 3385 NH2 ARG D 334 43.299 111.401 178.525 1.00 145.40 3386 C ARG D 334 37.378 112.727 182.841 1.00 5.42 3387 O ARG D 334 37.095 113.087 183.979 1.00 48.58 3388 N GLY D 335 37.273 111.473 182.444 1.00 20.86 3389 CA GLY D 335 36.759 110.464 183.343 1.00 41.07 3390 C GLY D 335 37.790 109.753 184.165 1.00 29.22 3391 O GLY D 335 38.979 109.833 183.880 1.00 46.30 3392 N VAL D 336 37.326 109.034 185.179 1.00 37.28 3393 CA VAL D 336 38.220 108.307 186.063 1.00 5.96 3394 CB VAL D 336 37.470 107.553 187.153 1.00 31.42 3395 CG1 VAL D 336 38.326 106.455 187.693 1.00 28.30 3396 CG2 VAL D 336 37.136 108.471 188.264 1.00 26.00 3397 C VAL D 336 39.053 107.302 185.328 1.00 38.88 3398 O VAL D 336 38.554 106.584 184.463 1.00 39.16 3399 N SER D 337 40.325 107.252 185.712 1.00 43.15 3400 CA SER D 337 41.306 106.342 185.141 1.00 54.37 3401 CB SER D 337 42.393 107.149 184.445 1.00 48.14 3402 OG SER D 337 41.836 108.240 183.724 1.00 87.47 3403 C SER D 337 41.904 105.601 186.321 1.00 32.96 3404 O SER D 337 41.957 106.143 187.413 1.00 38.71 3405 N ALA D 338 42.330 104.361 186.128 1.00 43.73 3406 CA ALA D 338 42.942 103.622 187.234 1.00 32.03 3407 CB ALA D 338 42.005 102.619 187.813 1.00 13.06 3408 C ALA D 338 44.176 102.928 186.739 1.00 38.96 3409 O ALA D 338 44.243 102.514 185.591 1.00 58.49 3410 N TYR D 339 45.148 102.798 187.626 1.00 53.04 3411 CA TYR D 339 46.417 102.195 187.298 1.00 41.03 3412 CB TYR D 339 47.422 103.306 187.101 1.00 30.65 3413 CG TYR D 339 46.976 104.376 186.120 1.00 5.42 3414 CD1 TYR D 339 46.755 105.677 186.536 1.00 64.60 3415 CE1 TYR D 339 46.456 106.687 185.625 1.00 68.13 3416 CD2 TYR D 339 46.873 104.104 184.765 1.00 66.56 3417 CE2 TYR D 339 46.575 105.104 183.851 1.00 42.43 3418 CZ TYR D 339 46.373 106.396 184.287 1.00 52.17 3419 OH TYR D 339 46.134 107.408 183.379 1.00 96.24 3420 C TYR D 339 46.835 101.285 188.439 1.00 48.87 3421 O TYR D 339 46.362 101.445 189.558 1.00 76.65 3422 N LEU D 340 47.730 100.345 188.175 1.00 64.84 3423 CA LEU D 340 48.140 99.410 189.213 1.00 61.58 3424 CB LEU D 340 47.263 98.177 189.122 1.00 18.16 3425 CG LEU D 340 47.443 97.047 190.119 1.00 25.80 3426 CD1 LEU D 340 47.122 97.518 191.509 1.00 65.83 3427 CD2 LEU D 340 46.525 95.915 189.742 1.00 77.47 3428 C LEU D 340 49.597 99.023 189.051 1.00 81.86 3429 O LEU D 340 49.935 98.238 188.174 1.00 80.36 3430 N SER D 341 50.456 99.560 189.912 1.00 80.46 3431 CA SER D 341 51.886 99.302 189.822 1.00 85.77 3432 CB SER D 341 52.656 100.405 190.549 1.00 101.32 3433 OG SER D 341 54.041 100.346 190.248 1.00 155.34 3434 C SER D 341 52.304 97.947 190.358 1.00 81.11 3435 O SER D 341 51.698 97.429 191.277 1.00 77.74 3436 N ARG D 342 53.355 97.388 189.766 1.00 106.18 3437 CA ARG D 342 53.912 96.091 190.150 1.00 44.48 3438 CB ARG D 342 54.380 95.361 188.892 1.00 103.52 3439 CG ARG D 342 55.115 96.289 187.906 1.00 146.45 3440 CD ARG D 342 55.845 95.557 186.765 1.00 148.55 3441 NE ARG D 342 54.964 95.031 185.722 1.00 106.07 3442 CZ ARG D 342 54.265 93.904 185.823 1.00 125.40 3443 NH1 ARG D 342 54.337 93.159 186.925 1.00 81.34 3444 NH2 ARG D 342 53.479 93.525 184.823 1.00 138.83 3445 C ARG D 342 55.100 96.277 191.117 1.00 93.34 3446 O ARG D 342 55.835 97.267 191.044 1.00 84.98 3447 N PRO D 343 55.309 95.312 192.025 1.00 51.92 3448 CD PRO D 343 54.613 94.020 192.055 1.00 46.08 3449 CA PRO D 343 56.390 95.336 193.017 1.00 37.46 3450 CB PRO D 343 56.323 93.946 193.638 1.00 54.05 3451 CG PRO D 343 54.925 93.534 193.435 1.00 34.48 3452 C PRO D 343 57.728 95.556 192.357 1.00 31.46 3453 O PRO D 343 58.023 94.920 191.352 1.00 83.41 3454 N SER D 344 58.555 96.430 192.906 1.00 68.87 3455 CA SER D 344 59.859 96.648 192.298 1.00 74.31 3456 CB SER D 344 60.476 97.969 192.781 1.00 78.99 3457 OG SER D 344 60.734 97.939 194.173 1.00 86.16 3458 C SER D 344 60.764 95.480 192.681 1.00 78.78 3459 O SER D 344 60.571 94.858 193.730 1.00 64.79 3460 N PRO D 345 61.744 95.149 191.822 1.00 78.82 3461 CD PRO D 345 62.114 95.844 190.579 1.00 86.56 3462 CA PRO D 345 62.673 94.054 192.096 1.00 69.52 3463 CB PRO D 345 63.792 94.311 191.101 1.00 81.00 3464 CG PRO D 345 63.078 94.883 189.947 1.00 56.65 3465 C PRO D 345 63.162 94.234 193.523 1.00 87.38 3466 O PRO D 345 63.009 93.356 194.382 1.00 70.47 3467 N PHE D 346 63.745 95.408 193.750 1.00 57.09 3468 CA PHE D 346 64.270 95.788 195.044 1.00 47.21 3469 CB PHE D 346 64.603 97.279 195.036 1.00 62.17 3470 CG PHE D 346 65.157 97.779 196.334 1.00 92.21 3471 CD1 PHE D 346 66.368 97.309 196.814 1.00 77.54 3472 CD2 PHE D 346 64.459 98.712 197.085 1.00 130.01 3473 CE1 PHE D 346 66.874 97.759 198.016 1.00 101.47 3474 CE2 PHE D 346 64.958 99.170 198.294 1.00 121.98 3475 CZ PHE D 346 66.167 98.693 198.761 1.00 136.63 3476 C PHE D 346 63.300 95.463 196.180 1.00 61.69 3477 O PHE D 346 63.557 94.562 196.976 1.00 58.05 3478 N ASP D 347 62.186 96.182 196.250 1.00 49.53 3479 CA ASP D 347 61.199 95.958 197.302 1.00 60.77 3480 CB ASP D 347 59.939 96.792 197.044 1.00 97.33 3481 CG ASP D 347 60.121 98.260 197.380 1.00 120.23 3482 OD1 ASP D 347 60.197 98.590 198.583 1.00 142.30 3483 OD2 ASP D 347 60.189 99.084 196.443 1.00 147.88 3484 C ASP D 347 60.791 94.494 197.407 1.00 79.99 3485 O ASP D 347 60.144 94.086 198.373 1.00 51.27 3486 N LEU D 348 61.191 93.697 196.427 1.00 54.00 3487 CA LEU D 348 60.791 92.304 196.400 1.00 73.58 3488 CB LEU D 348 60.293 91.977 194.991 1.00 43.65 3489 CG LEU D 348 59.764 90.586 194.663 1.00 61.62 3490 CD1 LEU D 348 58.851 90.063 195.737 1.00 73.74 3491 CD2 LEU D 348 59.041 90.673 193.342 1.00 84.11 3492 C LEU D 348 61.823 91.287 196.838 1.00 79.18 3493 O LEU D 348 61.456 90.240 197.381 1.00 67.98 3494 N PHE D 349 63.103 91.596 196.617 1.00 89.01 3495 CA PHE D 349 64.195 90.681 196.959 1.00 97.99 3496 CB PHE D 349 64.993 90.401 195.706 1.00 91.42 3497 CG PHE D 349 64.191 89.710 194.656 1.00 89.32 3498 CD1 PHE D 349 64.403 89.967 193.315 1.00 93.99 3499 CD2 PHE D 349 63.194 88.804 195.021 1.00 58.86 3500 CE1 PHE D 349 63.633 89.339 192.352 1.00 60.78 3501 CE2 PHE D 349 62.420 88.171 194.061 1.00 91.28 3502 CZ PHE D 349 62.639 88.439 192.724 1.00 94.91 3503 C PHE D 349 65.098 91.150 198.076 1.00 102.56 3504 O PHE D 349 65.470 90.369 198.955 1.00 116.27 3505 N ILE D 350 65.464 92.422 198.033 1.00 96.29 3506 CA ILE D 350 66.276 92.993 199.088 1.00 73.68 3507 CB ILE D 350 66.804 94.381 198.700 1.00 73.26 3508 CG2 ILE D 350 67.594 94.970 199.850 1.00 90.70 3509 CG1 ILE D 350 67.638 94.282 197.428 1.00 62.89 3510 CD1 ILE D 350 68.682 93.207 197.474 1.00 77.68 3511 C ILE D 350 65.337 93.162 200.286 1.00 91.79 3512 O ILE D 350 65.229 92.277 201.143 1.00 96.73 3513 N ARG D 351 64.639 94.299 200.302 1.00 79.05 3514 CA ARG D 351 63.696 94.661 201.356 1.00 77.91 3515 CB ARG D 351 62.908 95.894 200.909 1.00 81.92 3516 CG ARG D 351 62.429 96.796 202.033 1.00 114.59 3517 CD ARG D 351 62.218 98.216 201.513 1.00 129.04 3518 NE ARG D 351 61.772 99.135 202.556 1.00 176.58 3519 CZ ARG D 351 60.594 99.057 203.165 1.00 194.68 3520 NH1 ARG D 351 59.738 98.100 202.835 1.00 199.64 3521 NH2 ARG D 351 60.271 99.937 204.105 1.00 191.83 3522 C ARG D 351 62.738 93.529 201.737 1.00 87.28 3523 O ARG D 351 62.129 93.558 202.807 1.00 85.89 3524 N LYS D 352 62.620 92.536 200.860 1.00 64.64 3525 CA LYS D 352 61.754 91.375 201.066 1.00 110.09 3526 CB LYS D 352 62.443 90.351 201.977 1.00 137.68 3527 CG LYS D 352 63.695 89.710 201.380 1.00 164.74 3528 CD LYS D 352 64.045 88.410 202.099 1.00 184.77 3529 CE LYS D 352 65.381 87.834 201.642 1.00 171.68 3530 NZ LYS D 352 66.539 88.623 202.153 1.00 185.42 3531 C LYS D 352 60.339 91.659 201.587 1.00 121.79 3532 O LYS D 352 59.714 90.793 202.198 1.00 115.18 3533 N SER D 353 59.841 92.869 201.344 1.00 129.12 3534 CA SER D 353 58.484 93.265 201.740 1.00 107.18 3535 CB SER D 353 58.506 94.174 202.975 1.00 122.87 3536 OG SER D 353 59.158 95.404 202.707 1.00 166.93 3537 C SER D 353 57.907 94.012 200.534 1.00 102.01 3538 O SER D 353 57.957 95.243 200.446 1.00 86.01 3539 N PRO D 354 57.350 93.261 199.578 1.00 86.76 3540 CD PRO D 354 57.251 91.797 199.555 1.00 96.08 3541 CA PRO D 354 56.770 93.816 198.361 1.00 78.36 3542 CB PRO D 354 56.785 92.630 197.393 1.00 84.14 3543 CG PRO D 354 57.526 91.526 198.127 1.00 77.25 3544 C PRO D 354 55.367 94.332 198.547 1.00 94.58 3545 O PRO D 354 54.605 93.797 199.350 1.00 69.20 3546 N THR D 355 55.033 95.366 197.781 1.00 81.15 3547 CA THR D 355 53.706 95.957 197.813 1.00 52.66 3548 CB THR D 355 53.598 97.082 198.827 1.00 55.40 3549 OG1 THR D 355 54.557 98.101 198.513 1.00 77.41 3550 CG2 THR D 355 53.816 96.551 200.232 1.00 118.83 3551 C THR D 355 53.328 96.554 196.475 1.00 73.36 3552 O THR D 355 54.123 97.269 195.852 1.00 60.58 3553 N ILE D 356 52.100 96.261 196.054 1.00 68.63 3554 CA ILE D 356 51.550 96.771 194.809 1.00 71.72 3555 CB ILE D 356 50.725 95.712 194.105 1.00 33.12 3556 CG2 ILE D 356 51.621 94.618 193.613 1.00 84.96 3557 CG1 ILE D 356 49.693 95.138 195.059 1.00 69.76 3558 CD1 ILE D 356 48.895 93.992 194.466 1.00 78.12 3559 C ILE D 356 50.660 97.956 195.140 1.00 56.65 3560 O ILE D 356 50.092 98.020 196.214 1.00 40.32 3561 N THR D 357 50.527 98.886 194.210 1.00 41.53 3562 CA THR D 357 49.738 100.075 194.453 1.00 56.47 3563 CB THR D 357 50.661 101.268 194.609 1.00 44.57 3564 OG1 THR D 357 51.732 100.908 195.484 1.00 86.28 3565 CG2 THR D 357 49.919 102.440 195.180 1.00 70.27 3566 C THR D 357 48.719 100.390 193.367 1.00 61.21 3567 O THR D 357 49.043 100.408 192.182 1.00 65.37 3568 N CYS D 358 47.487 100.656 193.794 1.00 57.66 3569 CA CYS D 358 46.388 100.989 192.898 1.00 62.45 3570 C CYS D 358 46.155 102.478 192.983 1.00 45.63 3571 O CYS D 358 45.867 102.993 194.054 1.00 74.78 3572 CB CYS D 358 45.135 100.263 193.341 1.00 61.30 3573 SG CYS D 358 43.775 100.299 192.140 1.00 68.08 3574 N LEU D 359 46.272 103.174 191.864 1.00 41.70 3575 CA LEU D 359 46.105 104.616 191.868 1.00 25.08 3576 CB LEU D 359 47.404 105.279 191.410 1.00 65.10 3577 CG LEU D 359 47.322 106.716 190.905 1.00 16.89 3578 CD1 LEU D 359 46.716 107.566 191.963 1.00 57.67 3579 CD2 LEU D 359 48.703 107.229 190.549 1.00 96.64 3580 C LEU D 359 44.954 105.063 190.986 1.00 44.20 3581 O LEU D 359 44.956 104.830 189.784 1.00 68.36 3582 N VAL D 360 43.971 105.715 191.591 1.00 50.01 3583 CA VAL D 360 42.821 106.193 190.853 1.00 29.75 3584 CB VAL D 360 41.539 105.909 191.602 1.00 34.70 3585 CG1 VAL D 360 40.388 106.459 190.821 1.00 38.83 3586 CG2 VAL D 360 41.365 104.422 191.810 1.00 28.01 3587 C VAL D 360 42.927 107.681 190.661 1.00 28.40 3588 O VAL D 360 43.209 108.404 191.601 1.00 60.69 3589 N VAL D 361 42.677 108.146 189.450 1.00 28.27 3590 CA VAL D 361 42.771 109.574 189.156 1.00 32.16 3591 CB VAL D 361 44.007 109.853 188.272 1.00 10.08 3592 CG1 VAL D 361 44.974 108.690 188.387 1.00 49.51 3593 CG2 VAL D 361 43.595 110.013 186.820 1.00 48.77 3594 C VAL D 361 41.525 110.131 188.458 1.00 26.83 3595 O VAL D 361 40.695 109.389 187.937 1.00 48.72 3596 N ASP D 362 41.422 111.452 188.433 1.00 44.02 3597 CA ASP D 362 40.308 112.142 187.804 1.00 31.26 3598 CB ASP D 362 40.227 111.794 186.324 1.00 57.54 3599 CG ASP D 362 41.377 112.380 185.527 1.00 99.45 3600 OD1 ASP D 362 41.751 113.542 185.804 1.00 59.82 3601 OD2 ASP D 362 41.893 111.684 184.620 1.00 97.18 3602 C ASP D 362 38.945 111.946 188.458 1.00 45.28 3603 O ASP D 362 37.914 112.146 187.816 1.00 58.17 3604 N LEU D 363 38.943 111.554 189.730 1.00 31.65 3605 CA LEU D 363 37.709 111.405 190.496 1.00 30.37 3606 CB LEU D 363 37.964 110.712 191.820 1.00 14.90 3607 CG LEU D 363 38.139 109.208 191.819 1.00 39.19 3608 CD1 LEU D 363 38.611 108.750 193.177 1.00 47.04 3609 CD2 LEU D 363 36.839 108.553 191.480 1.00 35.75 3610 C LEU D 363 37.243 112.814 190.820 1.00 68.38 3611 O LEU D 363 38.045 113.751 190.805 1.00 53.90 3612 N ALA D 364 35.962 112.974 191.142 1.00 116.09 3613 CA ALA D 364 35.443 114.297 191.475 1.00 94.58 3614 CB ALA D 364 34.731 114.906 190.280 1.00 92.82 3615 C ALA D 364 34.498 114.228 192.656 1.00 118.54 3616 O ALA D 364 33.729 113.273 192.797 1.00 129.25 3617 N PRO D 365 34.548 115.252 193.524 1.00 128.97 3618 CD PRO D 365 35.391 116.455 193.354 1.00 57.81 3619 CA PRO D 365 33.710 115.360 194.723 1.00 105.98 3620 CB PRO D 365 33.666 116.860 194.958 1.00 121.84 3621 CG PRO D 365 35.087 117.254 194.616 1.00 78.18 3622 C PRO D 365 32.323 114.734 194.549 1.00 91.22 3623 O PRO D 365 31.436 115.298 193.916 1.00 85.50 3624 N SER D 366 32.162 113.542 195.107 1.00 132.49 3625 CA SER D 366 30.904 112.816 195.033 1.00 136.44 3626 CB SER D 366 31.149 111.400 194.503 1.00 121.82 3627 OG SER D 366 32.105 110.710 195.302 1.00 115.17 3628 C SER D 366 30.313 112.752 196.438 1.00 176.44 3629 O SER D 366 31.031 112.918 197.428 1.00 164.25 3630 N LYS D 367 29.007 112.523 196.524 1.00 189.75 3631 CA LYS D 367 28.341 112.430 197.819 1.00 181.41 3632 CB LYS D 367 26.896 112.910 197.720 1.00 196.81 3633 CG LYS D 367 26.739 114.334 197.233 1.00 225.05 3634 CD LYS D 367 27.059 115.373 198.291 1.00 212.98 3635 CE LYS D 367 26.738 116.763 197.760 1.00 208.48 3636 NZ LYS D 367 26.913 117.823 198.784 1.00 202.36 3637 C LYS D 367 28.355 110.982 198.274 1.00 162.45 3638 O LYS D 367 28.021 110.677 199.416 1.00 165.32 3639 N GLY D 368 28.735 110.093 197.365 1.00 160.80 3640 CA GLY D 368 28.791 108.685 197.696 1.00 152.04 3641 C GLY D 368 30.217 108.220 197.912 1.00 174.77 3642 O GLY D 368 31.174 108.928 197.582 1.00 170.78 3643 N THR D 369 30.355 107.023 198.476 1.00 173.28 3644 CA THR D 369 31.661 106.424 198.740 1.00 158.08 3645 CB THR D 369 31.492 105.030 199.398 1.00 168.98 3646 OG1 THR D 369 30.447 105.089 200.378 1.00 140.65 3647 CG2 THR D 369 32.788 104.590 200.079 1.00 155.41 3648 C THR D 369 32.375 106.253 197.396 1.00 126.97 3649 O THR D 369 31.908 106.754 196.380 1.00 121.57 3650 N VAL D 370 33.514 105.566 197.397 1.00 124.90 3651 CA VAL D 370 34.254 105.306 196.166 1.00 58.92 3652 CB VAL D 370 35.273 106.414 195.851 1.00 55.35 3653 CG1 VAL D 370 35.805 106.246 194.401 1.00 24.89 3654 CG2 VAL D 370 34.616 107.793 196.044 1.00 62.46 3655 C VAL D 370 34.955 103.979 196.320 1.00 27.33 3656 O VAL D 370 36.068 103.773 195.862 1.00 70.43 3657 N ASN D 371 34.256 103.075 196.988 1.00 82.80 3658 CA ASN D 371 34.734 101.724 197.243 1.00 69.31 3659 CB ASN D 371 33.595 100.719 196.996 1.00 49.52 3660 CG ASN D 371 32.950 100.229 198.274 1.00 104.67 3661 OD1 ASN D 371 32.407 101.025 199.043 1.00 117.80 3662 ND2 ASN D 371 32.979 98.919 198.497 1.00 168.88 3663 C ASN D 371 35.958 101.252 196.469 1.00 80.11 3664 O ASN D 371 35.988 101.271 195.234 1.00 50.10 3665 N LEU D 372 36.972 100.847 197.218 1.00 87.75 3666 CA LEU D 372 38.168 100.270 196.635 1.00 40.25 3667 CB LEU D 372 39.399 101.036 197.078 1.00 51.63 3668 CG LEU D 372 40.698 100.819 196.321 1.00 42.05 3669 CD1 LEU D 372 40.673 99.475 195.610 1.00 57.36 3670 CD2 LEU D 372 40.854 101.961 195.344 1.00 17.22 3671 C LEU D 372 38.164 98.893 197.302 1.00 69.49 3672 O LEU D 372 37.925 98.774 198.504 1.00 99.46 3673 N THR D 373 38.398 97.852 196.524 1.00 50.31 3674 CA THR D 373 38.367 96.516 197.078 1.00 38.63 3675 CB THR D 373 36.958 95.894 196.859 1.00 63.65 3676 OG1 THR D 373 35.980 96.704 197.523 1.00 71.89 3677 CG2 THR D 373 36.905 94.478 197.408 1.00 89.69 3678 C THR D 373 39.435 95.613 196.478 1.00 74.34 3679 O THR D 373 39.493 95.440 195.262 1.00 67.92 3680 N TRP D 374 40.273 95.032 197.335 1.00 71.85 3681 CA TRP D 374 41.343 94.148 196.885 1.00 42.08 3682 CB TRP D 374 42.566 94.309 197.769 1.00 57.45 3683 CG TRP D 374 43.280 95.595 197.614 1.00 41.03 3684 CD2 TRP D 374 44.219 95.924 196.593 1.00 30.13 3685 CE2 TRP D 374 44.648 97.244 196.827 1.00 32.56 3686 CE3 TRP D 374 44.740 95.229 195.500 1.00 52.50 3687 CD1 TRP D 374 43.176 96.697 198.410 1.00 58.12 3688 NE1 TRP D 374 44.000 97.697 197.944 1.00 31.82 3689 CZ2 TRP D 374 45.570 97.881 196.006 1.00 53.35 3690 CZ3 TRP D 374 45.658 95.864 194.684 1.00 47.95 3691 CH2 TRP D 374 46.064 97.175 194.939 1.00 23.35 3692 C TRP D 374 40.954 92.681 196.910 1.00 85.67 3693 O TRP D 374 40.261 92.236 197.822 1.00 80.11 3694 N SER D 375 41.434 91.916 195.936 1.00 64.91 3695 CA SER D 375 41.110 90.496 195.878 1.00 80.39 3696 CB SER D 375 39.737 90.325 195.236 1.00 121.93 3697 OG SER D 375 39.703 90.935 193.956 1.00 111.06 3698 C SER D 375 42.135 89.659 195.114 1.00 105.31 3699 O SER D 375 42.802 90.157 194.202 1.00 54.37 3700 N ARG D 376 42.253 88.386 195.493 1.00 87.71 3701 CA ARG D 376 43.174 87.466 194.831 1.00 90.92 3702 CB ARG D 376 43.974 86.665 195.854 1.00 101.35 3703 CG ARG D 376 45.158 87.402 196.423 1.00 114.89 3704 CD ARG D 376 46.249 86.437 196.863 1.00 123.05 3705 NE ARG D 376 46.021 85.871 198.187 1.00 92.73 3706 CZ ARG D 376 46.833 84.992 198.763 1.00 124.05 3707 NH1 ARG D 376 47.920 84.580 198.128 1.00 110.55 3708 NH2 ARG D 376 46.567 84.534 199.978 1.00 162.37 3709 C ARG D 376 42.420 86.499 193.927 1.00 117.75 3710 O ARG D 376 41.260 86.168 194.186 1.00 105.90 3711 N ALA D 377 43.082 86.039 192.871 1.00 99.06 3712 CA ALA D 377 42.453 85.109 191.944 1.00 110.56 3713 CB ALA D 377 43.235 85.059 190.659 1.00 96.70 3714 C ALA D 377 42.355 83.715 192.550 1.00 113.96 3715 O ALA D 377 41.454 82.940 192.218 1.00 121.96 3716 N SER D 378 43.288 83.400 193.441 1.00 100.05 3717 CA SER D 378 43.299 82.102 194.096 1.00 74.96 3718 CB SER D 378 44.607 81.910 194.863 1.00 108.91 3719 OG SER D 378 44.639 82.730 196.015 1.00 102.13 3720 C SER D 378 42.119 81.973 195.060 1.00 87.98 3721 O SER D 378 41.716 80.868 195.415 1.00 117.47 3722 N GLY D 379 41.569 83.105 195.478 1.00 88.22 3723 CA GLY D 379 40.452 83.080 196.403 1.00 101.70 3724 C GLY D 379 40.922 83.261 197.835 1.00 122.17 3725 O GLY D 379 40.135 83.578 198.733 1.00 104.23 3726 N LYS D 380 42.218 83.064 198.047 1.00 123.72 3727 CA LYS D 380 42.805 83.202 199.373 1.00 148.58 3728 CB LYS D 380 44.260 82.727 199.348 1.00 164.15 3729 CG LYS D 380 44.446 81.293 198.871 1.00 172.83 3730 CD LYS D 380 45.922 80.912 198.838 1.00 182.01 3731 CE LYS D 380 46.121 79.480 198.365 1.00 174.42 3732 NZ LYS D 380 47.562 79.099 198.345 1.00 158.73 3733 C LYS D 380 42.737 84.654 199.854 1.00 146.29 3734 O LYS D 380 43.016 85.582 199.096 1.00 155.06 3735 N PRO D 381 42.360 84.863 201.126 1.00 140.56 3736 CD PRO D 381 41.968 83.800 202.069 1.00 154.32 3737 CA PRO D 381 42.240 86.184 201.757 1.00 132.74 3738 CB PRO D 381 42.074 85.834 203.231 1.00 144.55 3739 CG PRO D 381 41.264 84.578 203.163 1.00 138.88 3740 C PRO D 381 43.428 87.119 201.507 1.00 118.02 3741 O PRO D 381 44.490 86.675 201.074 1.00 99.94 3742 N VAL D 382 43.239 88.410 201.793 1.00 105.18 3743 CA VAL D 382 44.279 89.429 201.584 1.00 80.19 3744 CB VAL D 382 43.901 90.375 200.458 1.00 64.06 3745 CG1 VAL D 382 43.890 89.629 199.140 1.00 134.59 3746 CG2 VAL D 382 42.530 90.963 200.739 1.00 87.60 3747 C VAL D 382 44.553 90.305 202.791 1.00 102.12 3748 O VAL D 382 43.654 90.583 203.581 1.00 116.29 3749 N ASN D 383 45.796 90.764 202.913 1.00 100.94 3750 CA ASN D 383 46.189 91.618 204.033 1.00 127.59 3751 CB ASN D 383 47.694 91.910 203.982 1.00 137.48 3752 CG ASN D 383 48.543 90.699 204.346 1.00 150.77 3753 OD1 ASN D 383 49.767 90.707 204.178 1.00 132.07 3754 ND2 ASN D 383 47.897 89.654 204.857 1.00 146.01 3755 C ASN D 383 45.411 92.928 203.998 1.00 88.67 3756 O ASN D 383 44.731 93.223 203.021 1.00 96.54 3757 N HIS D 384 45.510 93.708 205.068 1.00 90.17 3758 CA HIS D 384 44.810 94.985 205.142 1.00 76.61 3759 CB HIS D 384 44.747 95.464 206.594 1.00 88.84 3760 CG HIS D 384 43.971 94.546 207.492 1.00 115.42 3761 CD2 HIS D 384 44.367 93.491 208.244 1.00 119.90 3762 ND1 HIS D 384 42.602 94.630 207.639 1.00 93.91 3763 CE1 HIS D 384 42.189 93.665 208.443 1.00 115.01 3764 NE2 HIS D 384 43.239 92.960 208.823 1.00 139.25 3765 C HIS D 384 45.538 95.996 204.281 1.00 71.38 3766 O HIS D 384 46.757 96.000 204.219 1.00 48.03 3767 N SER D 385 44.787 96.859 203.617 1.00 81.66 3768 CA SER D 385 45.396 97.845 202.748 1.00 36.20 3769 CB SER D 385 44.638 97.893 201.424 1.00 66.21 3770 OG SER D 385 43.265 98.161 201.638 1.00 99.18 3771 C SER D 385 45.467 99.247 203.338 1.00 61.33 3772 O SER D 385 44.928 99.529 204.404 1.00 72.76 3773 N THR D 386 46.130 100.119 202.601 1.00 38.22 3774 CA THR D 386 46.341 101.507 202.949 1.00 30.42 3775 CB THR D 386 47.810 101.868 202.631 1.00 78.59 3776 OG1 THR D 386 48.625 101.545 203.761 1.00 109.39 3777 CG2 THR D 386 47.973 103.333 202.247 1.00 82.78 3778 C THR D 386 45.416 102.332 202.086 1.00 55.16 3779 O THR D 386 44.858 101.819 201.124 1.00 85.45 3780 N ARG D 387 45.240 103.608 202.412 1.00 60.12 3781 CA ARG D 387 44.399 104.459 201.569 1.00 57.26 3782 CB ARG D 387 42.956 104.032 201.709 1.00 45.25 3783 CG ARG D 387 41.990 104.919 200.996 1.00 58.55 3784 CD ARG D 387 40.661 104.219 200.838 1.00 62.37 3785 NE ARG D 387 39.669 105.097 200.233 1.00 75.16 3786 CZ ARG D 387 38.472 104.694 199.827 1.00 113.22 3787 NH1 ARG D 387 38.125 103.418 199.965 1.00 105.83 3788 NH2 ARG D 387 37.627 105.564 199.282 1.00 88.31 3789 C ARG D 387 44.528 105.952 201.834 1.00 49.54 3790 O ARG D 387 44.421 106.373 202.977 1.00 74.17 3791 N LYS D 388 44.759 106.743 200.784 1.00 14.61 3792 CA LYS D 388 44.909 108.195 200.915 1.00 49.64 3793 CB LYS D 383 46.349 108.672 200.653 1.00 19.49 3794 CG LYS D 388 47.490 107.749 201.074 1.00 148.66 3795 CD LYS D 388 48.839 108.366 200.675 1.00 145.63 3796 CE LYS D 388 50.016 107.483 201.069 1.00 169.40 3797 NZ LYS D 388 51.321 108.173 200.844 1.00 149.37 3798 C LYS D 388 44.068 108.854 199.854 1.00 40.50 3799 O LYS D 388 44.011 108.358 198.735 1.00 60.66 3800 N GLU D 389 43.425 109.971 200.183 1.00 34.31 3801 CA GLU D 389 42.645 110.713 199.183 1.00 51.61 3802 CB GLU D 389 41.143 110.672 199.478 1.00 15.19 3803 CG GLU D 389 40.520 109.280 199.334 1.00 140.73 3804 CD GLU D 389 39.070 109.211 199.796 1.00 168.49 3805 OE1 GLU D 389 38.263 110.060 199.354 1.00 149.55 3806 OE2 GLU D 389 38.741 108.300 200.594 1.00 151.07 3807 C GLU D 389 43.118 112.159 199.147 1.00 49.41 3808 O GLU D 389 42.719 112.969 199.973 1.00 85.28 3809 N GLU D 390 43.966 112.478 198.178 1.00 36.48 3810 CA GLU D 390 44.525 113.817 198.052 1.00 75.79 3811 CB GLU D 390 46.005 113.748 197.638 1.00 105.75 3812 CG GLU D 390 46.901 112.828 198.462 1.00 149.81 3813 CD GLU D 390 48.363 112.896 198.028 1.00 166.87 3814 OE1 GLU D 390 48.638 112.760 196.814 1.00 167.85 3815 OE2 GLU D 390 49.237 113.080 198.903 1.00 158.75 3816 C GLU D 390 43.826 114.727 197.055 1.00 24.22 3817 O GLU D 390 43.939 114.519 195.855 1.00 71.23 3818 N LYS D 391 43.126 115.746 197.535 1.00 39.14 3819 CA LYS D 391 42.485 116.689 196.620 1.00 57.00 3820 CB LYS D 391 41.731 117.794 197.388 1.00 45.82 3821 CG LYS D 391 41.324 118.992 196.519 1.00 82.77 3822 CD LYS D 391 41.375 120.325 197.271 1.00 142.55 3823 CE LYS D 391 40.285 120.453 198.331 1.00 170.58 3824 NZ LYS D 391 40.286 121.807 198.979 1.00 121.90 3825 C LYS D 391 43.652 117.317 195.856 1.00 48.81 3826 O LYS D 391 44.550 117.872 196.476 1.00 51.69 3827 N GLN D 392 43.649 117.218 194.526 1.00 65.02 3828 CA GLN D 392 44.730 117.787 193.725 1.00 59.17 3829 CB GLN D 392 44.920 116.991 192.448 1.00 65.61 3830 CG GLN D 392 45.169 115.537 192.684 1.00 54.54 3831 CD GLN D 392 46.454 115.307 193.399 1.00 38.88 3832 OE1 GLN D 392 46.604 115.681 194.556 1.00 126.60 3833 NE2 GLN D 392 47.412 114.693 192.712 1.00 107.57 3834 C GLN D 392 44.461 119.237 193.368 1.00 88.60 3835 O GLN D 392 43.348 119.743 193.559 1.00 64.57 3836 N ARG D 393 45.487 119.896 192.835 1.00 88.23 3837 CA ARG D 393 45.381 121.299 192.463 1.00 103.72 3838 CB ARG D 393 46.747 121.855 192.045 1.00 134.66 3839 CG ARG D 393 46.697 123.320 191.590 1.00 159.94 3840 CD ARG D 393 47.397 124.271 192.559 1.00 160.67 3841 NE ARG D 393 48.846 124.077 192.564 1.00 168.47 3842 CZ ARG D 393 49.702 124.859 193.212 1.00 172.58 3843 NH1 ARG D 393 49.257 125.894 193.913 1.00 174.62 3844 NH2 ARG D 393 51.004 124.606 193.160 1.00 174.39 3845 C ARG D 393 44.382 121.561 191.351 1.00 83.46 3846 O ARG D 393 43.633 122.543 191.414 1.00 96.92 3847 N ASN D 394 44.357 120.694 190.338 1.00 93.61 3848 CA ASN D 394 43.437 120.897 189.219 1.00 95.98 3849 CB ASN D 394 43.924 120.138 187.969 1.00 83.40 3850 CG ASN D 394 43.957 118.632 188.154 1.00 48.87 3851 OD1 ASN D 394 43.110 118.070 188.828 1.00 66.78 3852 ND2 ASN D 394 44.927 117.982 187.516 1.00 75.04 3853 C ASN D 394 41.952 120.583 189.479 1.00 59.45 3854 O ASN D 394 41.227 120.189 188.572 1.00 59.33 3855 N GLY D 395 41.494 120.775 190.710 1.00 79.33 3856 CA GLY D 395 40.099 120.509 191.008 1.00 71.67 3857 C GLY D 395 39.724 119.038 191.108 1.00 59.87 3858 O GLY D 395 38.677 118.700 191.669 1.00 74.71 3859 N THR D 396 40.564 118.157 190.574 1.00 62.74 3860 CA THR D 396 40.274 116.730 190.626 1.00 61.60 3861 CB THR D 396 41.206 115.932 189.705 1.00 47.87 3862 OG1 THR D 396 40.702 114.600 189.558 1.00 156.72 3863 CG2 THR D 396 42.599 115.848 190.305 1.00 112.24 3864 C THR D 396 40.436 116.198 192.048 1.00 53.86 3865 O THR D 396 40.495 116.964 193.001 1.00 71.70 3866 N LEU D 397 40.520 114.878 192.171 1.00 45.95 3867 CA LEU D 397 40.655 114.203 193.454 1.00 53.38 3868 CB LEU D 397 39.281 114.097 194.110 1.00 59.95 3869 CG LEU D 397 39.121 113.074 195.221 1.00 55.86 3870 CD1 LEU D 397 40.080 113.397 196.345 1.00 111.38 3871 CD2 LEU D 397 37.685 113.061 195.710 1.00 106.37 3872 C LEU D 397 41.232 112.809 193.198 1.00 50.48 3873 O LEU D 397 40.675 112.039 192.417 1.00 62.36 3874 N THR D 398 42.337 112.493 193.868 1.00 40.39 3875 CA THR D 398 43.020 111.224 193.706 1.00 21.97 3876 CB THR D 398 44.512 111.441 193.543 1.00 25.83 3877 OG1 THR D 398 44.756 112.125 192.315 1.00 66.94 3878 CG2 THR D 398 45.246 110.136 193.527 1.00 67.01 3879 C THR D 398 42.844 110.303 194.865 1.00 24.03 3880 O THR D 398 42.586 110.737 195.973 1.00 59.86 3881 N VAL D 399 43.008 109.015 194.602 1.00 37.39 3882 CA VAL D 399 42.909 107.980 195.628 1.00 37.07 3883 CB VAL D 399 41.574 107.254 195.564 1.00 32.64 3884 CG1 VAL D 399 41.609 106.041 196.480 1.00 32.87 3885 CG2 VAL D 399 40.476 108.176 195.946 1.00 28.21 3886 C VAL D 399 43.973 106.932 195.385 1.00 41.18 3887 O VAL D 399 44.031 106.372 194.293 1.00 45.84 3888 N THR D 400 44.818 106.664 196.375 1.00 50.23 3889 CA THR D 400 45.834 105.625 196.202 1.00 38.12 3890 CB THR D 400 47.270 106.128 196.319 1.00 43.92 3891 OG1 THR D 400 47.494 106.558 197.655 1.00 69.44 3892 CG2 THR D 400 47.526 107.280 195.375 1.00 45.17 3893 C THR D 400 45.648 104.626 197.309 1.00 35.51 3894 O THR D 400 45.223 104.968 198.404 1.00 64.95 3895 N SER D 401 45.969 103.382 197.016 1.00 42.58 3896 CA SER D 401 45.840 102.318 197.990 1.00 42.11 3897 CB SER D 401 44.515 101.584 197.833 1.00 59.45 3898 OG SER D 401 44.482 100.421 198.643 1.00 51.13 3899 C SER D 401 46.946 101.344 197.735 1.00 49.43 3900 O SER D 401 47.042 100.807 196.641 1.00 49.62 3901 N THR D 402 47.779 101.118 198.742 1.00 72.73 3902 CA THR D 402 48.894 100.196 198.624 1.00 50.60 3903 CB THR D 402 50.150 100.813 199.187 1.00 50.34 3904 OG1 THR D 402 50.322 102.117 198.630 1.00 61.02 3905 CG2 THR D 402 51.345 99.975 198.836 1.00 108.37 3906 C THR D 402 48.571 98.928 199.394 1.00 59.31 3907 O THR D 402 47.951 98.978 200.447 1.00 73.63 3908 N LEU D 403 48.995 97.790 198.872 1.00 60.48 3909 CA LEU D 403 48.701 96.520 199.510 1.00 51.40 3910 CB LEU D 403 47.648 95.785 198.689 1.00 60.86 3911 CG LEU D 403 47.239 94.398 199.166 1.00 71.08 3912 CD1 LEU D 403 46.519 94.506 200.492 1.00 115.39 3913 CD2 LEU D 403 46.339 93.757 198.140 1.00 75.16 3914 C LEU D 403 49.919 95.624 199.684 1.00 86.73 3915 O LEU D 403 50.684 95.411 198.741 1.00 48.79 3916 N PRO D 404 50.113 95.090 200.901 1.00 45.77 3917 CD PRO D 404 49.349 95.460 202.098 1.00 72.52 3918 CA PRO D 404 51.215 94.203 201.270 1.00 60.92 3919 CB PRO D 404 51.070 94.080 202.784 1.00 110.61 3920 CG PRO D 404 50.390 95.345 203.168 1.00 84.70 3921 C PRO D 404 51.030 92.861 200.573 1.00 78.31 3922 O PRO D 404 49.926 92.321 200.528 1.00 62.25 3923 N VAL D 405 52.116 92.304 200.055 1.00 85.38 3924 CA VAL D 405 52.015 91.056 199.330 1.00 72.08 3925 CB VAL D 405 52.032 91.358 197.832 1.00 42.37 3926 CG1 VAL D 405 53.051 90.497 197.120 1.00 129.72 3927 CG2 VAL D 405 50.651 91.145 197.266 1.00 97.10 3928 C VAL D 405 53.063 90.002 199.661 1.00 107.38 3929 O VAL D 405 54.263 90.289 199.721 1.00 92.57 3930 N GLY D 406 52.584 88.772 199.849 1.00 74.73 3931 CA GLY D 406 53.459 87.656 200.171 1.00 128.36 3932 C GLY D 406 54.503 87.396 199.084 1.00 128.26 3933 O GLY D 406 54.170 86.932 197.995 1.00 94.96 3934 N THR D 407 55.763 87.675 199.410 1.00 145.41 3935 CA THR D 407 56.880 87.505 198.508 1.00 103.78 3936 CB THR D 407 58.220 87.513 199.231 1.00 128.76 3937 OG1 THR D 407 58.109 88.244 200.452 1.00 153.49 3938 CG2 THR D 407 59.289 88.139 198.329 1.00 97.34 3939 C THR D 407 56.852 86.189 197.741 1.00 107.15 3940 O THR D 407 57.225 86.126 196.572 1.00 95.02 3941 N ARG D 408 56.441 85.123 198.408 1.00 126.42 3942 CA ARG D 408 56.399 83.820 197.772 1.00 134.10 3943 CB ARG D 408 56.112 82.750 198.816 1.00 151.42 3944 CG ARG D 408 57.188 82.649 199.914 1.00 177.48 3945 CD ARG D 408 57.344 83.945 200.730 1.00 172.46 3946 NE ARG D 408 56.196 84.229 201.588 1.00 159.11 3947 CZ ARG D 408 56.079 85.320 202.337 1.00 143.95 3948 NH1 ARG D 408 57.038 86.240 202.332 1.00 95.33 3949 NH2 ARG D 408 55.013 85.480 203.107 1.00 128.49 3950 C ARG D 408 55.302 83.805 196.723 1.00 126.54 3951 O ARG D 408 55.556 83.753 195.505 1.00 112.58 3952 N ASP D 409 54.070 83.869 197.211 1.00 115.25 3953 CA ASP D 409 52.874 83.849 196.382 1.00 99.87 3954 CB ASP D 409 51.731 84.516 197.160 1.00 106.74 3955 CG ASP D 409 51.541 83.939 198.559 1.00 132.42 3956 OD1 ASP D 409 51.021 82.808 198.688 1.00 129.76 3957 OD2 ASP D 409 51.909 84.625 199.539 1.00 112.17 3958 C ASP D 409 53.053 84.546 195.032 1.00 89.51 3959 O ASP D 409 52.675 84.000 193.990 1.00 130.58 3960 N TRP D 410 53.622 85.749 195.061 1.00 75.82 3961 CA TRP D 410 53.836 86.534 193.853 1.00 67.87 3962 CB TRP D 410 54.487 87.863 194.209 1.00 73.93 3963 CG TRP D 410 54.924 88.660 193.025 1.00 51.99 3964 CD2 TRP D 410 54.138 89.608 192.297 1.00 89.75 3965 CE2 TRP D 410 54.954 90.123 191.266 1.00 74.90 3966 CE3 TRP D 410 52.822 90.071 192.416 1.00 51.02 3967 CD1 TRP D 410 56.145 88.636 192.423 1.00 101.45 3968 NE1 TRP D 410 56.174 89.515 191.365 1.00 51.04 3969 CZ2 TRP D 410 54.498 91.083 190.357 1.00 99.21 3970 CZ3 TRP D 410 52.369 91.020 191.518 1.00 50.44 3971 CH2 TRP D 410 53.208 91.520 190.496 1.00 72.30 3972 C TRP D 410 54.684 85.829 192.825 1.00 97.87 3973 O TRP D 410 54.246 85.630 191.693 1.00 127.37 3974 N ILE D 411 55.900 85.458 193.215 1.00 107.01 3975 CA ILE D 411 56.807 84.797 192.283 1.00 114.82 3976 CB ILE D 411 58.125 84.422 192.943 1.00 90.18 3977 CG2 ILE D 411 59.219 84.374 191.890 1.00 113.38 3978 CG1 ILE D 411 58.504 85.477 193.973 1.00 122.60 3979 CD1 ILE D 411 59.713 85.112 194.782 1.00 160.55 3980 C ILE D 411 56.182 83.539 191.713 1.00 131.40 3981 O ILE D 411 56.470 83.146 190.585 1.00 115.52 3982 N GLU D 412 55.322 82.903 192.497 1.00 92.44 3983 CA GLU D 412 54.655 81.704 192.031 1.00 108.96 3984 CB GLU D 412 54.287 80.823 193.216 1.00 133.49 3985 CG GLU D 412 55.489 80.102 193.793 1.00 154.48 3986 CD GLU D 412 55.112 79.134 194.888 1.00 184.63 3987 OE1 GLU D 412 54.194 78.315 194.668 1.00 187.73 3988 OE2 GLU D 412 55.738 79.187 195.967 1.00 191.09 3989 C GLU D 412 53.428 81.997 191.162 1.00 137.18 3990 O GLU D 412 52.457 81.236 191.149 1.00 129.46 3991 N GLY D 413 53.485 83.118 190.446 1.00 164.33 3992 CA GLY D 413 52.417 83.501 189.535 1.00 162.77 3993 C GLY D 413 51.059 83.957 190.041 1.00 141.45 3994 O GLY D 413 50.144 84.149 189.237 1.00 136.83 3995 N GLU D 414 50.903 84.135 191.347 1.00 129.17 3996 CA GLU D 414 49.620 84.580 191.869 1.00 99.45 3997 CB GLU D 414 49.731 84.925 193.349 1.00 110.96 3998 CG GLU D 414 48.471 85.542 193.936 1.00 90.67 3999 CD GLU D 414 47.256 84.634 193.834 1.00 94.32 4000 OE1 GLU D 414 46.758 84.399 192.709 1.00 112.62 4001 OE2 GLU D 414 46.802 84.152 194.891 1.00 91.31 4002 C GLU D 414 49.146 85.803 191.098 1.00 100.87 4003 O GLU D 414 49.917 86.424 190.368 1.00 107.15 4004 N THR D 415 47.876 86.149 191.266 1.00 111.06 4005 CA THR D 415 47.303 87.291 190.574 1.00 112.82 4006 CB THR D 415 46.590 86.825 189.295 1.00 119.50 4007 OG1 THR D 415 45.583 87.773 188.933 1.00 115.11 4008 CG2 THR D 415 45.993 85.452 189.487 1.00 150.67 4009 C THR D 415 46.348 88.115 191.442 1.00 127.64 4010 O THR D 415 45.360 87.595 191.982 1.00 91.30 4011 N TYR D 416 46.664 89.407 191.559 1.00 114.78 4012 CA TYR D 416 45.899 90.360 192.366 1.00 69.47 4013 CB TYR D 416 46.846 91.150 193.276 1.00 76.73 4014 CG TYR D 416 47.732 90.297 194.155 1.00 89.68 4015 CD1 TYR D 416 48.988 89.875 193.724 1.00 115.56 4016 CE1 TYR D 416 49.787 89.049 194.524 1.00 52.64 4017 CD2 TYR D 416 47.298 89.877 195.406 1.00 74.22 4018 CE2 TYR D 416 48.086 89.054 196.210 1.00 65.75 4019 CZ TYR D 416 49.321 88.645 195.766 1.00 79.16 4020 OH TYR D 416 50.081 87.831 196.571 1.00 157.74 4021 C TYR D 416 45.089 91.342 191.521 1.00 92.20 4022 O TYR D 416 45.521 91.745 190.438 1.00 69.13 4023 N GLN D 417 43.931 91.752 192.037 1.00 67.36 4024 CA GLN D 417 43.050 92.668 191.319 1.00 48.33 4025 CB GLN D 417 41.897 91.876 190.709 1.00 124.19 4026 CG GLN D 417 41.057 92.649 189.718 1.00 145.26 4027 CD GLN D 417 39.854 91.857 189.256 1.00 138.49 4028 OE1 GLN D 417 38.942 91.590 190.037 1.00 121.32 4029 NE2 GLN D 417 39.848 91.469 187.985 1.00 129.85 4030 C GLN D 417 42.484 93.795 192.191 1.00 57.83 4031 O GLN D 417 42.091 93.579 193.338 1.00 77.99 4032 N CYS D 418 42.426 94.992 191.614 1.00 66.84 4033 CA CYS D 418 41.930 96.191 192.286 1.00 48.93 4034 C CYS D 418 40.585 96.549 191.670 1.00 61.50 4035 O CYS D 418 40.496 96.739 190.465 1.00 67.84 4036 CB CYS D 418 42.927 97.336 192.079 1.00 66.08 4037 SG CYS D 418 42.483 98.904 192.868 1.00 95.99 4038 N ARG D 419 39.541 96.638 192.490 1.00 50.79 4039 CA ARG D 419 38.201 96.969 191.992 1.00 30.24 4040 CB ARG D 419 37.226 95.822 192.284 1.00 108.73 4041 CG ARG D 419 35.835 96.025 191.697 1.00 188.65 4042 CD ARG D 419 34.860 94.941 192.125 1.00 228.92 4043 NE ARG D 419 33.561 95.099 191.473 1.00 243.94 4044 CZ ARG D 419 32.495 94.354 191.738 1.00 230.39 4045 NH1 ARG D 419 32.566 93.394 192.649 1.00 220.71 4046 NH2 ARG D 419 31.359 94.565 191.090 1.00 214.39 4047 C ARG D 419 37.661 98.255 192.610 1.00 69.76 4048 O ARG D 419 37.299 98.287 193.797 1.00 59.29 4049 N VAL D 420 37.597 99.315 191.809 1.00 18.00 4050 CA VAL D 420 37.074 100.578 192.324 1.00 56.50 4051 CB VAL D 420 37.934 101.774 191.866 1.00 52.22 4052 CG1 VAL D 420 39.318 101.315 191.544 1.00 42.61 4053 CG2 VAL D 420 37.327 102.441 190.689 1.00 35.59 4054 C VAL D 420 35.665 100.745 191.782 1.00 35.00 4055 O VAL D 420 35.385 100.297 190.700 1.00 37.99 4056 N THR D 421 34.772 101.395 192.502 1.00 56.57 4057 CA THR D 421 33.425 101.562 191.982 1.00 23.71 4058 CB THR D 421 32.465 100.554 192.642 1.00 45.48 4059 OG1 THR D 421 32.418 100.794 194.052 1.00 67.88 4060 CG2 THR D 421 32.941 99.141 192.431 1.00 34.10 4061 C THR D 421 32.981 102.971 192.327 1.00 45.43 4062 O THR D 421 33.240 103.446 193.427 1.00 48.61 4063 N HIS D 422 32.334 103.649 191.389 1.00 43.04 4064 CA HIS D 422 31.840 105.009 191.627 1.00 50.66 4065 CB HIS D 422 32.559 106.002 190.718 1.00 14.59 4066 CG HIS D 422 32.154 107.422 190.931 1.00 21.53 4067 CD2 HIS D 422 32.698 108.580 190.485 1.00 65.88 4068 ND1 HIS D 422 31.052 107.779 191.675 1.00 53.72 4069 CE1 HIS D 422 30.935 109.095 191.681 1.00 114.73 4070 NE2 HIS D 422 31.922 109.606 190.966 1.00 87.07 4071 C HIS D 422 30.344 105.008 191.319 1.00 73.12 4072 O HIS D 422 29.920 104.610 190.236 1.00 67.37 4073 N PRO D 423 29.523 105.465 192.265 1.00 58.08 4074 CD PRO D 423 29.888 106.227 193.469 1.00 54.31 4075 CA PRO D 423 28.076 105.492 192.059 1.00 71.43 4076 CB PRO D 423 27.608 106.488 193.108 1.00 46.51 4077 CG PRO D 423 28.588 106.285 194.211 1.00 82.86 4078 C PRO D 423 27.619 105.884 190.654 1.00 63.28 4079 O PRO D 423 26.833 105.173 190.028 1.00 81.37 4080 N HIS D 424 28.123 107.005 190.157 1.00 34.90 4081 CA HIS D 424 27.730 107.502 188.848 1.00 59.77 4082 CB HIS D 424 28.010 108.999 188.754 1.00 37.61 4083 CG HIS D 424 27.748 109.743 190.019 1.00 60.94 4084 CD2 HIS D 424 27.244 109.336 191.207 1.00 98.42 4085 ND1 HIS D 424 28.068 111.072 190.174 1.00 78.59 4086 CE1 HIS D 424 27.778 111.452 191.406 1.00 152.64 4087 NE2 HIS D 424 27.277 110.417 192.054 1.00 152.52 4088 C HIS D 424 28.388 106.814 187.654 1.00 36.89 4089 O HIS D 424 28.568 107.433 186.612 1.00 54.52 4090 N LEU D 425 28.758 105.548 187.776 1.00 21.15 4091 CA LEU D 425 29.371 104.884 186.632 1.00 37.06 4092 CB LEU D 425 30.857 104.611 186.893 1.00 56.98 4093 CG LEU D 425 31.771 105.825 187.067 1.00 23.50 4094 CD1 LEU D 425 33.179 105.368 187.366 1.00 58.60 4095 CD2 LEU D 425 31.746 106.677 185.827 1.00 24.67 4096 C LEU D 425 28.680 103.584 186.237 1.00 31.46 4097 O LEU D 425 28.161 102.858 187.077 1.00 64.74 4098 N PRO D 426 28.660 103.287 184.936 1.00 23.81 4099 CD PRO D 426 29.067 104.203 183.862 1.00 71.59 4100 CA PRO D 426 28.053 102.088 184.376 1.00 41.36 4101 CB PRO D 426 28.260 102.281 182.885 1.00 29.87 4102 CG PRO D 426 28.215 103.739 182.734 1.00 66.78 4103 C PRO D 426 28.735 100.834 184.912 1.00 26.52 4104 O PRO D 426 28.315 100.289 185.916 1.00 55.27 4105 N ARG D 427 29.785 100.369 184.249 1.00 73.53 4106 CA ARG D 427 30.472 99.182 184.725 1.00 63.70 4107 CB ARG D 427 31.083 98.404 183.541 1.00 62.24 4108 CG ARG D 427 30.616 96.941 183.493 1.00 74.02 4109 CD ARG D 427 31.214 96.127 182.354 1.00 70.65 4110 NE ARG D 427 31.336 94.711 182.718 1.00 159.98 4111 CZ ARG D 427 31.878 93.762 181.953 1.00 164.46 4112 NH1 ARG D 427 32.363 94.046 180.749 1.00 124.37 4113 NH2 ARG D 427 31.951 92.516 182.405 1.00 133.62 4114 C ARG D 427 31.532 99.618 185.751 1.00 86.41 4115 O ARG D 427 31.880 100.800 185.828 1.00 47.25 4116 N ALA D 428 32.013 98.674 186.559 1.00 93.41 4117 CA ALA D 428 33.005 98.970 187.595 1.00 41.66 4118 CB ALA D 428 32.956 97.912 188.669 1.00 102.75 4119 C ALA D 428 34.400 99.058 187.028 1.00 45.06 4120 O ALA D 428 34.674 98.543 185.958 1.00 75.62 4121 N LEU D 429 35.291 99.721 187.744 1.00 66.10 4122 CA LEU D 429 36.641 99.848 187.242 1.00 43.45 4123 CB LEU D 429 37.222 101.217 187.556 1.00 34.38 4124 CG LEU D 429 37.745 101.978 186.364 1.00 66.23 4125 CD1 LEU D 429 38.458 103.214 186.845 1.00 46.80 4126 CD2 LEU D 429 38.672 101.084 185.569 1.00 115.61 4127 C LEU D 429 37.484 98.785 187.887 1.00 54.85 4128 O LEU D 429 37.496 98.631 189.117 1.00 59.59 4129 N MET D 430 38.184 98.040 187.043 1.00 47.43 4130 CA MET D 430 39.057 96.962 187.494 1.00 53.01 4131 CB MET D 430 38.412 95.594 187.284 1.00 40.35 4132 CG MET D 430 37.179 95.375 188.128 1.00 77.82 4133 SD MET D 430 36.525 93.713 187.975 1.00 126.20 4134 CE MET D 430 35.574 93.859 186.419 1.00 161.71 4135 C MET D 430 40.366 96.986 186.745 1.00 63.35 4136 O MET D 430 40.448 97.480 185.612 1.00 42.39 4137 N ARG D 431 41.392 96.466 187.407 1.00 36.33 4138 CA ARG D 431 42.719 96.379 186.841 1.00 58.15 4139 CB ARG D 431 43.464 97.696 186.993 1.00 27.19 4140 CG ARG D 431 42.683 98.900 186.503 1.00 33.53 4141 CD ARG D 431 43.552 99.896 185.806 1.00 43.03 4142 NE ARG D 431 43.438 99.788 184.355 1.00 95.31 4143 CZ ARG D 431 42.328 100.067 183.679 1.00 104.17 4144 NH1 ARG D 431 41.245 100.468 184.330 1.00 37.36 4145 NH2 ARG D 431 42.300 99.949 182.355 1.00 165.84 4146 C ARG D 431 43.363 95.299 187.666 1.00 67.38 4147 O ARG D 431 43.050 95.151 188.839 1.00 56.89 4148 N SER D 432 44.240 94.527 187.046 1.00 77.67 4149 CA SER D 432 44.897 93.431 187.734 1.00 64.82 4150 CB SER D 432 44.192 92.118 187.410 1.00 56.74 4151 OG SER D 432 44.290 91.820 186.027 1.00 99.74 4152 C SER D 432 46.343 93.350 187.291 1.00 94.30 4153 O SER D 432 46.754 94.039 186.355 1.00 64.60 4154 N THR D 433 47.112 92.507 187.969 1.00 73.10 4155 CA THR D 433 48.519 92.339 187.647 1.00 82.03 4156 CB THR D 433 49.341 93.538 188.076 1.00 73.97 4157 OG1 THR D 433 50.696 93.368 187.640 1.00 108.43 4158 CG2 THR D 433 49.314 93.664 189.589 1.00 50.90 4159 C THR D 433 49.110 91.140 188.340 1.00 97.97 4160 O THR D 433 48.687 90.772 189.450 1.00 54.76 4161 N THR D 434 50.101 90.543 187.673 1.00 88.14 4162 CA THR D 434 50.835 89.377 188.176 1.00 61.31 4163 CB THR D 434 50.212 88.050 187.757 1.00 73.67 4164 OG1 THR D 434 50.604 87.723 186.414 1.00 136.86 4165 CG2 THR D 434 48.713 88.120 187.813 1.00 65.49 4166 C THR D 434 52.219 89.389 187.548 1.00 93.47 4167 O THR D 434 52.500 90.185 186.661 1.00 68.59 4168 N LYS D 435 53.052 88.481 188.041 1.00 104.82 4169 CA LYS D 435 54.425 88.280 187.620 1.00 97.19 4170 CB LYS D 435 54.913 86.952 188.190 1.00 108.47 4171 CG LYS D 435 56.289 86.406 187.805 1.00 156.78 4172 CD LYS D 435 56.494 85.099 188.627 1.00 153.33 4173 CE LYS D 435 57.777 84.278 188.369 1.00 171.23 4174 NZ LYS D 435 57.958 83.976 186.919 1.00 182.18 4175 C LYS D 435 54.554 88.263 186.100 1.00 93.46 4176 O LYS D 435 53.814 87.555 185.412 1.00 120.14 4177 N THR D 436 55.489 89.042 185.566 1.00 71.73 4178 CA THR D 436 55.677 89.079 184.118 1.00 82.60 4179 CB THR D 436 56.715 90.111 183.748 1.00 75.56 4180 OG1 THR D 436 56.400 91.352 184.383 1.00 131.33 4181 CG2 THR D 436 56.746 90.317 182.254 1.00 83.66 4182 C THR D 436 56.132 87.718 183.594 1.00 127.18 4183 O THR D 436 56.943 87.046 184.224 1.00 131.75 4184 N SER D 437 55.651 87.344 182.413 1.00 129.98 4185 CA SER D 437 55.976 86.043 181.824 1.00 150.36 4186 CB SER D 437 54.732 85.467 181.140 1.00 156.11 4187 OG SER D 437 54.249 86.345 180.132 1.00 150.74 4188 C SER D 437 57.136 86.032 180.844 1.00 145.33 4189 O SER D 437 57.791 87.049 180.633 1.00 128.92 4190 N GLY D 438 57.385 84.861 180.261 1.00 143.82 4191 CA GLY D 438 58.455 84.708 179.289 1.00 129.59 4192 C GLY D 438 59.692 83.989 179.804 1.00 109.80 4193 O GLY D 438 59.641 83.339 180.849 1.00 90.90 4194 N PRO D 439 60.814 84.057 179.066 1.00 96.86 4195 CD PRO D 439 60.853 84.528 177.672 1.00 102.41 4196 CA PRO D 439 62.088 83.431 179.427 1.00 112.86 4197 CB PRO D 439 62.754 83.224 178.079 1.00 143.69 4198 CG PRO D 439 62.322 84.442 177.338 1.00 120.60 4199 C PRO D 439 62.861 84.406 180.312 1.00 120.63 4200 O PRO D 439 62.881 85.600 180.044 1.00 129.73 4201 N ARG D 440 63.503 83.905 181.357 1.00 110.84 4202 CA ARG D 440 64.231 84.774 182.276 1.00 110.52 4203 CB ARG D 440 64.025 84.289 183.711 1.00 128.23 4204 CG ARG D 440 62.627 83.749 184.002 1.00 153.84 4205 CD ARG D 440 61.579 84.849 184.102 1.00 188.47 4206 NE ARG D 440 60.232 84.332 183.856 1.00 215.81 4207 CZ ARG D 440 59.122 84.806 184.410 1.00 224.86 4208 NH1 ARG D 440 59.180 85.822 185.260 1.00 223.24 4209 NH2 ARG D 440 57.954 84.257 184.108 1.00 209.34 4210 C ARG D 440 65.726 84.853 181.978 1.00 83.55 4211 O ARG D 440 66.468 83.937 182.310 1.00 129.96 4212 N ALA D 441 66.172 85.951 181.372 1.00 74.53 4213 CA ALA D 441 67.589 86.119 181.054 1.00 78.06 4214 CB ALA D 441 67.753 86.473 179.593 1.00 98.44 4215 C ALA D 441 68.222 87.195 181.922 1.00 73.89 4216 O ALA D 441 67.781 88.340 181.908 1.00 87.18 4217 N ALA D 442 69.267 86.818 182.659 1.00 108.00 4218 CA ALA D 442 69.993 87.722 183.560 1.00 84.59 4219 CB ALA D 442 71.104 86.959 184.254 1.00 124.78 4220 C ALA D 442 70.561 88.989 182.906 1.00 90.01 4221 O ALA D 442 70.706 89.070 181.687 1.00 88.98 4222 N PRO D 443 70.904 89.993 183.725 1.00 81.16 4223 CD PRO D 443 70.625 90.055 185.162 1.00 58.29 4224 CA PRO D 443 71.449 91.273 183.272 1.00 65.44 4225 CB PRO D 443 71.044 92.255 184.377 1.00 62.14 4226 CG PRO D 443 70.143 91.467 185.294 1.00 84.05 4227 C PRO D 443 72.943 91.293 183.088 1.00 72.84 4228 O PRO D 443 73.682 90.606 183.789 1.00 105.86 4229 N GLU D 444 73.376 92.113 182.145 1.00 79.19 4230 CA GLU D 444 74.782 92.292 181.855 1.00 104.43 4231 CB GLU D 444 75.063 92.051 180.370 1.00 143.96 4232 CG GLU D 444 75.062 90.591 179.943 1.00 170.26 4233 CD GLU D 444 74.905 90.425 178.443 1.00 152.52 4234 OE1 GLU D 444 75.481 91.243 177.693 1.00 116.93 4235 OE2 GLU D 444 74.210 89.475 178.018 1.00 138.72 4236 C GLU D 444 74.992 93.747 182.180 1.00 84.83 4237 O GLU D 444 74.317 94.602 181.616 1.00 95.04 4238 N VAL D 445 75.902 94.043 183.097 1.00 87.28 4239 CA VAL D 445 76.152 95.433 183.453 1.00 76.03 4240 CB VAL D 445 75.736 95.706 184.897 1.00 75.27 4241 CG1 VAL D 445 76.170 94.563 185.778 1.00 68.09 4242 CG2 VAL D 445 76.333 97.020 185.366 1.00 93.41 4243 C VAL D 445 77.599 95.863 183.264 1.00 60.53 4244 O VAL D 445 78.520 95.096 183.545 1.00 92.85 4245 N TYR D 446 77.791 97.090 182.783 1.00 65.90 4246 CA TYR D 446 79.128 97.633 182.546 1.00 97.21 4247 CB TYR D 446 79.483 97.555 181.054 1.00 115.92 4248 CG TYR D 446 79.187 96.214 180.416 1.00 124.25 4249 CD1 TYR D 446 78.088 96.048 179.579 1.00 108.68 4250 CE1 TYR D 446 77.774 94.803 179.036 1.00 143.50 4251 CD2 TYR D 446 79.975 95.097 180.692 1.00 175.81 4252 CE2 TYR D 446 79.671 93.845 180.153 1.00 164.42 4253 CZ TYR D 446 78.568 93.707 179.329 1.00 149.93 4254 OH TYR D 446 78.246 92.473 178.813 1.00 162.97 4255 C TYR D 446 79.143 99.086 182.995 1.00 97.06 4256 O TYR D 446 78.386 99.896 182.470 1.00 99.04 4257 N ALA D 447 80.005 99.415 183.956 1.00 102.47 4258 CA ALA D 447 80.100 100.782 184.484 1.00 66.24 4259 CB ALA D 447 80.300 100.730 185.984 1.00 89.68 4260 C ALA D 447 81.211 101.615 183.841 1.00 84.25 4261 O ALA D 447 82.290 101.102 183.544 1.00 81.08 4262 N PHE D 448 80.957 102.906 183.642 1.00 53.71 4263 CA PHE D 448 81.955 103.767 183.018 1.00 96.40 4264 CB PHE D 448 81.528 104.081 181.583 1.00 110.89 4265 CG PHE D 448 81.356 102.852 180.729 1.00 139.15 4266 CD1 PHE D 448 80.213 102.073 180.831 1.00 147.96 4267 CD2 PHE D 448 82.368 102.438 179.872 1.00 185.33 4268 CE1 PHE D 448 80.080 100.901 180.100 1.00 149.26 4269 CE2 PHE D 448 82.246 101.267 179.135 1.00 184.09 4270 CZ PHE D 448 81.099 100.497 179.250 1.00 182.71 4271 C PHE D 448 82.240 105.047 183.799 1.00 83.02 4272 O PHE D 448 81.778 105.196 184.921 1.00 92.98 4273 N ALA D 449 83.011 105.963 183.216 1.00 86.20 4274 CA ALA D 449 83.363 107.210 183.901 1.00 46.82 4275 CB ALA D 449 84.286 106.910 185.063 1.00 99.13 4276 C ALA D 449 84.019 108.243 182.987 1.00 66.70 4277 O ALA D 449 85.007 107.964 182.302 1.00 82.28 4278 N THR D 450 83.478 109.452 183.017 1.00 46.07 4279 CA THR D 450 83.953 110.551 182.182 1.00 90.49 4280 CB THR D 450 82.895 111.677 182.176 1.00 66.00 4281 OG1 THR D 450 81.684 111.176 181.611 1.00 102.05 4282 CG2 THR D 450 83.355 112.870 181.373 1.00 103.25 4283 C THR D 450 85.298 111.169 182.568 1.00 89.86 4284 O THR D 450 85.722 111.083 183.711 1.00 116.46 4285 N PRO D 451 86.004 111.760 181.590 1.00 87.34 4286 CD PRO D 451 85.899 111.307 180.196 1.00 73.15 4287 CA PRO D 451 87.298 112.421 181.800 1.00 105.99 4288 CB PRO D 451 87.997 112.253 180.450 1.00 127.70 4289 CG PRO D 451 87.335 111.052 179.859 1.00 115.43 4290 C PRO D 451 86.971 113.891 182.083 1.00 101.34 4291 O PRO D 451 85.922 114.375 181.670 1.00 107.89 4292 N GLU D 452 87.850 114.611 182.768 1.00 115.89 4293 CA GLU D 452 87.560 116.009 183.060 1.00 133.25 4294 CB GLU D 452 88.700 116.645 183.863 1.00 159.83 4295 CG GLU D 452 90.046 116.683 183.155 1.00 194.80 4296 CD GLU D 452 91.097 117.446 183.947 1.00 196.79 4297 OE1 GLU D 452 90.906 118.663 184.170 1.00 177.79 4298 OE2 GLU D 452 92.110 116.830 184.347 1.00 195.58 4299 C GLU D 452 87.294 116.834 181.801 1.00 120.67 4300 O GLU D 452 87.544 116.392 180.677 1.00 86.09 4301 N TRP D 453 86.776 118.039 182.007 1.00 123.90 4302 CA TRP D 453 86.462 118.953 180.916 1.00 145.95 4303 CB TRP D 453 84.992 118.777 180.504 1.00 170.02 4304 CG TRP D 453 84.500 119.744 179.459 1.00 197.51 4305 CD2 TRP D 453 84.449 119.528 178.042 1.00 214.10 4306 CE2 TRP D 453 83.925 120.703 177.457 1.00 215.96 4307 CE3 TRP D 453 84.792 118.453 177.210 1.00 219.72 4308 CD1 TRP D 453 84.022 121.006 179.668 1.00 209.18 4309 NE1 TRP D 453 83.675 121.589 178.471 1.00 210.81 4310 CZ2 TRP D 453 83.741 120.838 176.076 1.00 220.86 4311 CZ3 TRP D 453 84.609 118.587 175.834 1.00 220.01 4312 CH2 TRP D 453 84.086 119.772 175.284 1.00 223.85 4313 C TRP D 453 86.731 120.387 181.372 1.00 158.31 4314 O TRP D 453 86.448 120.748 182.517 1.00 155.59 4315 N PRO D 454 87.295 121.221 180.480 1.00 164.35 4316 CD PRO D 454 87.673 120.851 179.102 1.00 146.83 4317 CA PRO D 454 87.624 122.628 180.746 1.00 184.14 4318 CB PRO D 454 87.864 123.187 179.348 1.00 181.33 4319 CG PRO D 454 88.523 122.033 178.664 1.00 173.35 4320 C PRO D 454 86.558 123.418 181.509 1.00 195.45 4321 O PRO D 454 86.855 124.447 182.116 1.00 210.90 4322 N GLY D 455 85.321 122.934 181.474 1.00 201.41 4323 CA GLY D 455 84.239 123.613 182.165 1.00 189.27 4324 C GLY D 455 84.373 123.555 183.674 1.00 182.16 4325 O GLY D 455 84.142 124.550 184.362 1.00 191.75 4326 N SER D 456 84.746 122.388 184.189 1.00 171.47 4327 CA SER D 456 84.913 122.193 185.625 1.00 166.50 4328 CB SER D 456 83.591 121.774 186.261 1.00 158.47 4329 OG SER D 456 83.188 120.511 185.764 1.00 140.37 4330 C SER D 456 85.943 121.101 185.858 1.00 166.83 4331 O SER D 456 85.996 120.122 185.114 1.00 174.49 4332 N ARG D 457 86.751 121.264 186.899 1.00 175.34 4333 CA ARG D 457 87.787 120.288 187.213 1.00 178.26 4334 CB ARG D 457 89.137 121.000 187.387 1.00 185.27 4335 CG ARG D 457 89.546 121.846 186.184 1.00 203.14 4336 CD ARG D 457 90.908 122.507 186.373 1.00 206.79 4337 NE ARG D 457 91.246 123.379 185.247 1.00 216.85 4338 CZ ARG D 457 92.393 124.041 185.125 1.00 205.77 4339 NH1 ARG D 457 93.328 123.937 186.060 1.00 207.14 4340 NH2 ARG D 457 92.603 124.814 184.068 1.00 185.77 4341 C ARG D 457 87.468 119.472 188.464 1.00 162.65 4342 O ARG D 457 88.291 118.675 188.915 1.00 168.22 4343 N ASP D 458 86.274 119.660 189.018 1.00 149.08 4344 CA ASP D 458 85.890 118.934 190.226 1.00 166.05 4345 CB ASP D 458 85.908 119.875 191.434 1.00 188.82 4346 CG ASP D 458 87.300 120.382 191.754 1.00 202.29 4347 OD1 ASP D 458 88.212 119.544 191.919 1.00 202.70 4348 OD2 ASP D 458 87.480 121.615 191.843 1.00 197.86 4349 C ASP D 458 84.531 118.249 190.137 1.00 167.63 4350 O ASP D 458 83.930 117.904 191.158 1.00 106.20 4351 N LYS D 459 84.055 118.053 188.912 1.00 184.87 4352 CA LYS D 459 82.773 117.395 188.672 1.00 167.70 4353 CB LYS D 459 81.697 118.424 188.295 1.00 177.88 4354 CG LYS D 459 81.395 119.467 189.373 1.00 201.66 4355 CD LYS D 459 80.275 120.423 188.944 1.00 187.25 4356 CE LYS D 459 79.958 121.446 190.038 1.00 173.49 4357 NZ LYS D 459 78.840 122.362 189.668 1.00 145.56 4358 C LYS D 459 82.932 116.382 187.538 1.00 165.68 4359 O LYS D 459 83.276 116.748 186.410 1.00 172.64 4360 N ARG D 460 82.697 115.109 187.843 1.00 154.79 4361 CA ARG D 460 82.804 114.051 186.841 1.00 153.22 4362 CB ARG D 460 84.095 113.244 187.058 1.00 125.90 4363 CG ARG D 460 85.358 114.037 186.706 1.00 137.80 4364 CD ARG D 460 86.588 113.151 186.537 1.00 147.84 4365 NE ARG D 460 87.717 113.902 185.989 1.00 154.85 4366 CZ ARG D 460 88.857 113.355 185.572 1.00 177.19 4367 NH1 ARG D 460 89.037 112.042 185.634 1.00 158.76 4368 NH2 ARG D 460 89.824 114.124 185.090 1.00 193.89 4369 C ARG D 460 81.561 113.141 186.828 1.00 141.33 4370 O ARG D 460 81.033 112.758 187.876 1.00 118.12 4371 N THR D 461 81.116 112.794 185.623 1.00 106.56 4372 CA THR D 461 79.912 111.998 185.408 1.00 72.86 4373 CB THR D 461 79.214 112.496 184.135 1.00 85.08 4374 OG1 THR D 461 79.268 113.928 184.100 1.00 106.27 4375 CG2 THR D 461 77.771 112.026 184.092 1.00 59.78 4376 C THR D 461 80.058 110.484 185.278 1.00 72.76 4377 O THR D 461 80.940 110.002 184.571 1.00 64.16 4378 N LEU D 462 79.174 109.739 185.941 1.00 67.15 4379 CA LEU D 462 79.176 108.269 185.838 1.00 93.90 4380 CB LEU D 462 79.119 107.581 187.202 1.00 54.53 4381 CG LEU D 462 80.338 107.682 188.115 1.00 86.30 4382 CD1 LEU D 462 80.306 106.517 189.095 1.00 67.24 4383 CD2 LEU D 462 81.621 107.639 187.305 1.00 77.87 4384 C LEU D 462 77.991 107.767 185.029 1.00 86.86 4385 O LEU D 462 76.949 108.418 184.974 1.00 135.96 4386 N ALA D 463 78.158 106.600 184.416 1.00 84.07 4387 CA ALA D 463 77.117 105.982 183.597 1.00 70.48 4388 CB ALA D 463 77.311 106.345 182.132 1.00 69.52 4389 C ALA D 463 77.176 104.476 183.773 1.00 66.61 4390 O ALA D 463 78.250 103.897 183.916 1.00 72.40 4391 N CYS D 464 76.021 103.837 183.750 1.00 69.61 4392 CA CYS D 464 75.980 102.407 183.946 1.00 72.19 4393 C CYS D 464 74.947 101.799 183.022 1.00 95.42 4394 O CYS D 464 73.769 102.144 183.080 1.00 118.74 4395 CB CYS D 464 75.636 102.132 185.398 1.00 50.48 4396 SG CYS D 464 75.624 100.393 185.919 1.00 118.72 4397 N LEU D 465 75.400 100.890 182.167 1.00 95.81 4398 CA LEU D 465 74.530 100.233 181.207 1.00 80.91 4399 CB LEU D 465 75.167 100.288 179.824 1.00 62.17 4400 CG LEU D 465 74.700 99.281 178.772 1.00 81.47 4401 CD1 LEU D 465 73.187 99.193 178.728 1.00 87.06 4402 CD2 LEU D 465 75.254 99.711 177.427 1.00 84.82 4403 C LEU D 465 74.198 98.791 181.565 1.00 79.74 4404 O LEU D 465 75.083 97.957 181.726 1.00 54.90 4405 N ILE D 466 72.906 98.509 181.669 1.00 64.80 4406 CA ILE D 466 72.437 97.182 182.007 1.00 58.32 4407 CB ILE D 466 71.567 97.232 183.254 1.00 77.30 4408 CG2 ILE D 466 71.276 95.823 183.747 1.00 58.46 4409 CG1 ILE D 466 72.281 98.066 184.316 1.00 44.32 4410 CD1 ILE D 466 71.633 98.043 185.670 1.00 83.41 4411 C ILE D 466 71.624 96.670 180.837 1.00 93.77 4412 O ILE D 466 70.586 97.243 180.502 1.00 98.80 4413 N GLN D 467 72.087 95.590 180.215 1.00 97.61 4414 CA GLN D 467 71.385 95.063 179.060 1.00 69.11 4415 CB GLN D 467 72.115 95.487 177.796 1.00 36.98 4416 CG GLN D 467 73.590 95.168 177.789 1.00 80.17 4417 CD GLN D 467 74.224 95.357 176.419 1.00 115.95 4418 OE1 GLN D 467 74.035 96.388 175.759 1.00 80.89 4419 NE2 GLN D 467 74.989 94.359 175.986 1.00 133.96 4420 C GLN D 467 71.124 93.570 178.994 1.00 43.59 4421 O GLN D 467 71.414 92.816 179.917 1.00 51.62 4422 N ASN D 468 70.542 93.175 177.868 1.00 84.41 4423 CA ASN D 468 70.204 91.797 177.562 1.00 78.87 4424 CB ASN D 468 71.448 91.071 177.072 1.00 91.58 4425 CG ASN D 468 72.167 91.847 175.992 1.00 131.22 4426 OD1 ASN D 468 71.557 92.267 175.000 1.00 109.30 4427 ND2 ASN D 468 73.467 92.052 176.179 1.00 130.02 4428 C ASN D 468 69.571 91.050 178.709 1.00 94.97 4429 O ASN D 468 70.049 89.988 179.113 1.00 113.94 4430 N PHE D 469 68.487 91.609 179.236 1.00 56.14 4431 CA PHE D 469 67.783 90.960 180.327 1.00 70.60 4432 CB PHE D 469 68.001 91.710 181.643 1.00 43.17 4433 CG PHE D 469 67.537 93.134 181.619 1.00 94.42 4434 CD1 PHE D 469 66.376 93.509 182.276 1.00 47.15 4435 CD2 PHE D 469 68.280 94.110 180.968 1.00 95.42 4436 CE1 PHE D 469 65.962 94.836 182.290 1.00 103.25 4437 CE2 PHE D 469 67.877 95.441 180.978 1.00 28.33 4438 CZ PHE D 469 66.716 95.804 181.639 1.00 101.58 4439 C PHE D 469 66.308 90.888 180.020 1.00 67.94 4440 O PHE D 469 65.834 91.535 179.083 1.00 51.85 4441 N MET D 470 65.600 90.078 180.805 1.00 27.30 4442 CA MET D 470 64.158 89.910 180.673 1.00 69.57 4443 CB MET D 470 63.814 89.320 179.308 1.00 108.06 4444 CG MET D 470 64.665 88.140 178.901 1.00 121.33 4445 SD MET D 470 64.817 88.077 177.103 1.00 132.64 4446 CE MET D 470 63.162 87.566 176.645 1.00 170.43 4447 C MET D 470 63.637 89.020 181.785 1.00 73.39 4448 O MET D 470 64.295 88.068 182.173 1.00 72.89 4449 N PRO D 471 62.445 89.328 182.328 1.00 77.22 4450 CD PRO D 471 61.921 88.464 183.393 1.00 79.25 4451 CA PRO D 471 61.500 90.415 182.042 1.00 73.03 4452 CB PRO D 471 60.443 90.228 183.117 1.00 77.74 4453 CG PRO D 471 60.456 88.748 183.334 1.00 95.61 4454 C PRO D 471 62.108 91.805 182.094 1.00 66.54 4455 O PRO D 471 63.298 91.962 182.323 1.00 79.62 4456 N GLU D 472 61.280 92.819 181.886 1.00 87.24 4457 CA GLU D 472 61.768 94.188 181.907 1.00 83.72 4458 CB GLU D 472 60.933 95.063 180.969 1.00 104.73 4459 CG GLU D 472 59.432 95.001 181.206 1.00 166.05 4460 CD GLU D 472 58.686 96.116 180.490 1.00 187.22 4461 OE1 GLU D 472 58.879 96.275 179.267 1.00 172.24 4462 OE2 GLU D 472 57.904 96.834 181.149 1.00 193.81 4463 C GLU D 472 61.770 94.796 183.304 1.00 104.32 4464 O GLU D 472 62.261 95.906 183.487 1.00 102.37 4465 N ASP D 473 61.233 94.077 184.288 1.00 59.56 4466 CA ASP D 473 61.187 94.593 185.649 1.00 92.12 4467 CB ASP D 473 60.234 93.756 186.504 1.00 116.46 4468 CG ASP D 473 58.789 93.929 186.094 1.00 135.25 4469 OD1 ASP D 473 58.358 95.090 185.944 1.00 150.62 4470 OD2 ASP D 473 58.086 92.910 185.927 1.00 137.23 4471 C ASP D 473 62.564 94.620 186.291 1.00 79.36 4472 O ASP D 473 63.061 93.592 186.742 1.00 60.87 4473 N ILE D 474 63.163 95.805 186.359 1.00 77.86 4474 CA ILE D 474 64.493 95.947 186.935 1.00 57.62 4475 CB ILE D 474 65.541 96.119 185.823 1.00 72.84 4476 CG2 ILE D 474 65.559 97.554 185.331 1.00 52.57 4477 CG1 ILE D 474 66.933 95.793 186.346 1.00 77.16 4478 CD1 ILE D 474 68.003 95.929 185.283 1.00 68.46 4479 C ILE D 474 64.646 97.117 187.900 1.00 75.73 4480 O ILE D 474 64.083 98.194 187.689 1.00 80.08 4481 N SER D 475 65.427 96.893 188.952 1.00 67.18 4482 CA SER D 475 65.698 97.914 189.957 1.00 72.99 4483 CB SER D 475 65.258 97.429 191.351 1.00 63.48 4484 OG SER D 475 63.999 97.964 191.727 1.00 93.55 4485 C SER D 475 67.188 98.261 189.979 1.00 53.66 4486 O SER D 475 68.017 97.470 190.419 1.00 75.03 4487 N VAL D 476 67.521 99.448 189.499 1.00 55.61 4488 CA VAL D 476 68.902 99.906 189.483 1.00 51.07 4489 CB VAL D 476 69.166 100.775 188.240 1.00 63.18 4490 CG1 VAL D 476 70.539 101.424 188.313 1.00 61.47 4491 CG2 VAL D 476 69.062 99.927 187.005 1.00 79.72 4492 C VAL D 476 69.166 100.749 190.728 1.00 58.51 4493 O VAL D 476 68.232 101.248 191.346 1.00 116.08 4494 N GLN D 477 70.436 100.908 191.085 1.00 70.31 4495 CA GLN D 477 70.840 101.706 192.242 1.00 86.47 4496 CB GLN D 477 70.317 101.076 193.526 1.00 59.72 4497 CG GLN D 477 70.614 99.603 193.661 1.00 61.26 4498 CD GLN D 477 69.958 99.013 194.889 1.00 111.88 4499 OE1 GLN D 477 68.738 99.086 195.044 1.00 120.03 4500 NE2 GLN D 477 70.761 98.429 195.775 1.00 97.73 4501 C GLN D 477 72.355 101.845 192.331 1.00 83.04 4502 O GLN D 477 73.095 101.333 191.489 1.00 85.92 4503 N TRP D 478 72.829 102.546 193.349 1.00 78.76 4504 CA TRP D 478 74.264 102.706 193.495 1.00 100.96 4505 CB TRP D 478 74.714 104.068 192.967 1.00 36.74 4506 CG TRP D 478 74.440 104.322 191.529 1.00 63.43 4507 CD2 TRP D 478 75.397 104.315 190.457 1.00 64.22 4508 CE2 TRP D 478 74.751 104.834 189.318 1.00 63.92 4509 CE3 TRP D 478 76.742 103.930 190.355 1.00 92.35 4510 CD1 TRP D 478 73.285 104.799 191.002 1.00 69.30 4511 NE1 TRP D 478 73.461 105.120 189.676 1.00 83.14 4512 CZ2 TRP D 478 75.402 104.985 188.088 1.00 106.36 4513 CZ3 TRP D 478 77.391 104.080 189.132 1.00 74.82 4514 CH2 TRP D 478 76.719 104.606 188.016 1.00 79.83 4515 C TRP D 478 74.723 102.569 194.938 1.00 79.39 4516 O TRP D 478 73.959 102.797 195.866 1.00 116.11 4517 N LEU D 479 75.982 102.200 195.113 1.00 66.99 4518 CA LEU D 479 76.560 102.055 196.428 1.00 70.32 4519 CB LEU D 479 76.867 100.593 196.694 1.00 83.07 4520 CG LEU D 479 75.686 99.688 196.347 1.00 60.88 4521 CD1 LEU D 479 76.079 98.229 196.566 1.00 143.46 4522 CD2 LEU D 479 74.497 100.046 197.202 1.00 93.52 4523 C LEU D 479 77.834 102.878 196.431 1.00 94.55 4524 O LEU D 479 78.361 103.209 195.371 1.00 87.16 4525 N HIS D 480 78.323 103.214 197.619 1.00 131.47 4526 CA HIS D 480 79.537 104.013 197.746 1.00 117.34 4527 CB HIS D 480 79.249 105.474 197.383 1.00 110.78 4528 CG HIS D 480 80.387 106.413 197.658 1.00 107.86 4529 CD2 HIS D 480 80.407 107.644 198.226 1.00 112.04 4530 ND1 HIS D 480 81.683 106.156 197.264 1.00 95.10 4531 CE1 HIS D 480 82.449 107.187 197.572 1.00 106.89 4532 NE2 HIS D 480 81.698 108.104 198.156 1.00 113.38 4533 C HIS D 480 80.068 103.931 199.157 1.00 92.28 4534 O HIS D 480 79.612 104.647 200.049 1.00 92.69 4535 N ASN D 481 81.028 103.043 199.362 1.00 97.73 4536 CA ASN D 481 81.609 102.894 200.677 1.00 121.93 4537 CB ASN D 481 82.125 104.254 201.160 1.00 108.49 4538 CG ASN D 481 83.258 104.126 202.145 1.00 147.00 4539 OD1 ASN D 481 83.876 105.120 202.522 1.00 154.08 4540 ND2 ASN D 481 83.542 102.897 202.570 1.00 166.29 4541 C ASN D 481 80.546 102.355 201.630 1.00 81.70 4542 O ASN D 481 80.382 102.854 202.746 1.00 102.35 4543 N GLU D 482 79.817 101.342 201.169 1.00 78.94 4544 CA GLU D 482 78.776 100.706 201.975 1.00 126.14 4545 CB GLU D 482 79.365 100.258 203.324 1.00 135.98 4546 CG GLU D 482 80.643 99.421 203.217 1.00 152.58 4547 CD GLU D 482 80.427 98.088 202.517 1.00 174.16 4548 OE1 GLU D 482 79.638 97.265 203.030 1.00 170.45 4549 OE2 GLU D 482 81.047 97.863 201.455 1.00 174.56 4550 C GLU D 482 77.575 101.627 202.215 1.00 109.93 4551 O GLU D 482 76.820 101.447 203.175 1.00 82.30 4552 N VAL D 483 77.392 102.605 201.336 1.00 76.74 4553 CA VAL D 483 76.287 103.551 201.477 1.00 102.62 4554 CB VAL D 483 76.815 104.983 201.744 1.00 109.65 4555 CG1 VAL D 483 75.669 105.986 201.713 1.00 98.68 4556 CG2 VAL D 483 77.519 105.028 203.088 1.00 170.08 4557 C VAL D 483 75.392 103.588 200.243 1.00 117.05 4558 O VAL D 483 75.779 104.119 199.202 1.00 143.84 4559 N GLN D 484 74.193 103.027 200.365 1.00 104.30 4560 CA GLN D 484 73.244 103.003 199.258 1.00 63.80 4561 CB GLN D 484 72.062 102.112 199.617 1.00 106.13 4562 CG GLN D 484 71.037 101.964 198.510 1.00 90.87 4563 CD GLN D 484 69.823 101.181 198.969 1.00 129.10 4564 OE1 GLN D 484 69.946 100.156 199.659 1.00 95.62 4565 NE2 GLN D 484 68.639 101.654 198.587 1.00 134.96 4566 C GLN D 484 72.750 104.413 198.969 1.00 52.20 4567 O GLN D 484 71.799 104.874 199.588 1.00 109.44 4568 N LEU D 485 73.377 105.098 198.024 1.00 55.15 4569 CA LEU D 485 72.991 106.471 197.711 1.00 71.69 4570 CB LEU D 485 73.698 106.961 196.447 1.00 66.01 4571 CG LEU D 485 75.216 107.146 196.541 1.00 75.22 4572 CD1 LEU D 485 75.661 108.084 195.431 1.00 81.39 4573 CD2 LEU D 485 75.604 107.739 197.885 1.00 111.54 4574 C LEU D 485 71.504 106.758 197.579 1.00 78.22 4575 O LEU D 485 70.698 105.854 197.350 1.00 76.73 4576 N PRO D 486 71.127 108.040 197.735 1.00 77.50 4577 CD PRO D 486 72.025 109.127 198.161 1.00 119.22 4578 CA PRO D 486 69.749 108.532 197.646 1.00 96.61 4579 CB PRO D 486 69.876 110.004 198.038 1.00 131.87 4580 CG PRO D 486 71.086 110.026 198.916 1.00 136.66 4581 C PRO D 486 69.179 108.380 196.244 1.00 92.91 4582 O PRO D 486 69.756 108.858 195.264 1.00 55.14 4583 N ASP D 487 68.027 107.731 196.163 1.00 82.83 4584 CA ASP D 487 67.380 107.504 194.888 1.00 93.17 4585 CB ASP D 487 65.947 107.016 195.124 1.00 115.19 4586 CG ASP D 487 65.437 106.130 193.996 1.00 161.24 4587 OD1 ASP D 487 65.248 106.640 192.869 1.00 164.95 4588 OD2 ASP D 487 65.232 104.918 194.235 1.00 171.27 4589 C ASP D 487 67.383 108.752 193.995 1.00 74.98 4590 O ASP D 487 67.617 108.660 192.791 1.00 95.57 4591 N ALA D 488 67.149 109.920 194.583 1.00 74.62 4592 CA ALA D 488 67.100 111.162 193.812 1.00 77.13 4593 CB ALA D 488 66.474 112.268 194.656 1.00 113.89 4594 C ALA D 488 68.455 111.622 193.277 1.00 89.67 4595 O ALA D 488 68.559 112.683 192.647 1.00 78.05 4596 N ARG D 489 69.489 110.822 193.520 1.00 47.18 4597 CA ARG D 489 70.837 111.159 193.065 1.00 81.70 4598 CB ARG D 489 71.856 110.474 193.974 1.00 98.18 4599 CG ARG D 489 72.159 111.254 195.231 1.00 119.10 4600 CD ARG D 489 73.301 112.214 194.975 1.00 108.85 4601 NE ARG D 489 74.572 111.660 195.432 1.00 107.43 4602 CZ ARG D 489 75.764 112.102 195.042 1.00 115.63 4603 NH1 ARG D 489 75.858 113.107 194.175 1.00 102.89 4604 NH2 ARG D 489 76.863 111.548 195.532 1.00 113.00 4605 C ARG D 489 71.146 110.806 191.606 1.00 93.41 4606 O ARG D 489 71.879 111.526 190.920 1.00 91.06 4607 N HIS D 490 70.579 109.699 191.138 1.00 91.66 4608 CA HIS D 490 70.810 109.230 189.784 1.00 79.10 4609 CB HIS D 490 71.330 107.809 189.831 1.00 61.88 4610 CG HIS D 490 70.361 106.847 190.429 1.00 50.09 4611 CD2 HIS D 490 69.154 106.414 189.998 1.00 71.95 4612 ND1 HIS D 490 70.600 106.198 191.622 1.00 80.99 4613 CE1 HIS D 490 69.582 105.403 191.899 1.00 81.13 4614 NE2 HIS D 490 68.691 105.516 190.929 1.00 120.64 4615 C HIS D 490 69.567 109.238 188.925 1.00 73.38 4616 O HIS D 490 68.455 109.193 189.431 1.00 83.57 4617 N SER D 491 69.773 109.267 187.616 1.00 106.32 4618 CA SER D 491 68.676 109.246 186.663 1.00 99.85 4619 CB SER D 491 68.783 110.424 185.696 1.00 80.79 4620 OG SER D 491 67.681 110.437 184.802 1.00 153.32 4621 C SER D 491 68.731 107.937 185.879 1.00 95.44 4622 O SER D 491 69.712 107.647 185.204 1.00 77.44 4623 N THR D 492 67.678 107.140 185.974 1.00 107.33 4624 CA THR D 492 67.638 105.879 185.254 1.00 88.96 4625 CB THR D 492 67.385 104.714 186.217 1.00 93.46 4626 OG1 THR D 492 68.540 104.532 187.044 1.00 95.38 4627 CG2 THR D 492 67.093 103.435 185.453 1.00 86.11 4628 C THR D 492 66.529 105.932 184.216 1.00 97.57 4629 O THR D 492 65.418 106.361 184.520 1.00 115.51 4630 N THR D 493 66.826 105.501 182.993 1.00 66.72 4631 CA THR D 493 65.820 105.527 181.936 1.00 75.38 4632 CB THR D 493 66.444 105.482 180.543 1.00 81.55 4633 OG1 THR D 493 66.925 104.157 180.285 1.00 66.75 4634 CG2 THR D 493 67.587 106.470 180.445 1.00 83.27 4635 C THR D 493 64.856 104.354 182.017 1.00 88.44 4636 O THR D 493 64.911 103.529 182.941 1.00 70.82 4637 N GLN D 494 63.964 104.296 181.036 1.00 95.57 4638 CA GLN D 494 62.988 103.229 180.976 1.00 86.74 4639 CB GLN D 494 61.641 103.773 180.491 1.00 104.79 4640 CG GLN D 494 61.002 104.821 181.399 1.00 121.61 4641 CD GLN D 494 60.761 104.317 182.821 1.00 154.81 4642 OE1 GLN D 494 60.297 103.194 183.027 1.00 127.19 4643 NE2 GLN D 494 61.064 105.158 183.806 1.00 163.95 4644 C GLN D 494 63.500 102.163 180.014 1.00 105.68 4645 O GLN D 494 64.174 102.473 179.029 1.00 117.51 4646 N PRO D 495 63.204 100.889 180.301 1.00 74.85 4647 CD PRO D 495 62.540 100.401 181.518 1.00 68.14 4648 CA PRO D 495 63.620 99.765 179.469 1.00 67.40 4649 CB PRO D 495 62.844 98.607 180.069 1.00 57.90 4650 CG PRO D 495 62.886 98.927 181.501 1.00 51.00 4651 C PRO D 495 63.295 99.968 177.996 1.00 77.06 4652 O PRO D 495 62.317 100.621 177.647 1.00 102.71 4653 N ARG D 496 64.136 99.410 177.138 1.00 110.77 4654 CA ARG D 496 63.956 99.496 175.697 1.00 122.60 4655 CB ARG D 496 64.765 100.668 175.128 1.00 143.51 4656 CG ARG D 496 64.080 102.027 175.280 1.00 154.62 4657 CD ARG D 496 65.003 103.174 174.882 1.00 172.80 4658 NE ARG D 496 64.275 104.427 174.686 1.00 206.30 4659 CZ ARG D 496 63.560 104.716 173.603 1.00 204.90 4660 NH1 ARG D 496 63.477 103.842 172.608 1.00 198.29 4661 NH2 ARG D 496 62.923 105.877 173.515 1.00 192.83 4662 C ARG D 496 64.426 98.170 175.119 1.00 131.58 4663 O ARG D 496 65.365 97.568 175.630 1.00 107.54 4664 N LYS D 497 63.767 97.707 174.063 1.00 139.06 4665 CA LYS D 497 64.114 96.427 173.459 1.00 98.97 4666 CB LYS D 497 62.936 95.900 172.636 1.00 111.63 4667 CG LYS D 497 61.645 95.750 173.428 1.00 148.53 4668 CD LYS D 497 60.515 95.187 172.575 1.00 162.48 4669 CE LYS D 497 59.221 95.078 173.374 1.00 159.87 4670 NZ LYS D 497 58.111 94.478 172.579 1.00 147.14 4671 C LYS D 497 65.360 96.466 172.594 1.00 102.21 4672 O LYS D 497 65.804 97.525 172.155 1.00 87.29 4673 N THR D 498 65.919 95.287 172.358 1.00 121.14 4674 CA THR D 498 67.108 95.144 171.536 1.00 136.22 4675 CB THR D 498 68.350 94.851 172.400 1.00 124.43 4676 OG1 THR D 498 68.079 93.769 173.302 1.00 102.03 4677 CG2 THR D 498 68.724 96.073 173.194 1.00 135.22 4678 C THR D 498 66.928 94.020 170.520 1.00 160.20 4679 O THR D 498 66.064 93.148 170.677 1.00 127.05 4680 N LYS D 499 67.746 94.045 169.473 1.00 148.81 4681 CA LYS D 499 67.665 93.030 168.436 1.00 167.95 4682 CB LYS D 499 68.518 93.442 167.227 1.00 183.82 4683 CG LYS D 499 68.240 92.635 165.953 1.00 194.67 4684 CD LYS D 499 68.915 93.247 164.723 1.00 178.66 4685 CE LYS D 499 68.530 92.509 163.439 1.00 166.21 4686 NZ LYS D 499 69.080 93.166 162.212 1.00 129.82 4687 C LYS D 499 68.131 91.685 168.993 1.00 174.78 4688 O LYS D 499 68.477 90.773 168.243 1.00 193.59 4689 N GLY D 500 68.132 91.570 170.318 1.00 172.34 4690 CA GLY D 500 68.549 90.339 170.963 1.00 167.96 4691 C GLY D 500 67.489 89.841 171.925 1.00 174.62 4692 O GLY D 500 67.796 89.121 172.875 1.00 180.27 4693 N SER D 501 66.244 90.244 171.674 1.00 149.85 4694 CA SER D 501 65.086 89.863 172.485 1.00 145.87 4695 CB SER D 501 64.828 88.355 172.379 1.00 150.97 4696 OG SER D 501 65.865 87.601 172.983 1.00 182.29 4697 C SER D 501 65.171 90.255 173.960 1.00 148.85 4698 O SER D 501 64.317 89.871 174.758 1.00 131.95 4699 N GLY D 502 66.194 91.018 174.322 1.00 141.68 4700 CA GLY D 502 66.334 91.439 175.703 1.00 99.20 4701 C GLY D 502 66.210 92.943 175.805 1.00 120.83 4702 O GLY D 502 66.192 93.629 174.781 1.00 107.61 4703 N PHE D 503 66.121 93.465 177.027 1.00 106.97 4704 CA PHE D 503 66.005 94.906 177.208 1.00 87.81 4705 CB PHE D 503 64.911 95.253 178.201 1.00 59.57 4706 CG PHE D 503 63.595 94.625 177.908 1.00 73.29 4707 CD1 PHE D 503 63.264 93.397 178.453 1.00 86.43 4708 CD2 PHE D 503 62.658 95.290 177.144 1.00 53.84 4709 CE1 PHE D 503 62.015 92.845 178.250 1.00 84.48 4710 CE2 PHE D 503 61.404 94.747 176.932 1.00 115.27 4711 CZ PHE D 503 61.081 93.520 177.490 1.00 109.78 4712 C PHE D 503 67.293 95.543 177.700 1.00 86.70 4713 O PHE D 503 68.236 94.851 178.074 1.00 68.11 4714 N PHE D 504 67.304 96.874 177.720 1.00 64.93 4715 CA PHE D 504 68.463 97.628 178.160 1.00 58.80 4716 CB PHE D 504 69.399 97.867 176.972 1.00 62.27 4717 CG PHE D 504 69.039 99.068 176.119 1.00 49.02 4718 CD1 PHE D 504 69.470 100.338 176.467 1.00 69.40 4719 CD2 PHE D 504 68.314 98.916 174.948 1.00 92.30 4720 CE1 PHE D 504 69.192 101.431 175.665 1.00 83.85 4721 CE2 PHE D 504 68.030 100.006 174.138 1.00 117.28 4722 CZ PHE D 504 68.474 101.266 174.498 1.00 115.08 4723 C PHE D 504 68.066 98.962 178.779 1.00 67.09 4724 O PHE D 504 67.236 99.690 178.233 1.00 100.63 4725 N VAL D 505 68.662 99.283 179.920 1.00 82.59 4726 CA VAL D 505 68.376 100.546 180.583 1.00 86.93 4727 CB VAL D 505 67.554 100.339 181.865 1.00 66.93 4728 CG1 VAL D 505 68.374 99.626 182.909 1.00 44.42 4729 CG2 VAL D 505 67.089 101.683 182.388 1.00 110.77 4730 C VAL D 505 69.672 101.266 180.936 1.00 63.33 4731 O VAL D 505 70.685 100.634 181.212 1.00 81.80 4732 N PHE D 506 69.629 102.592 180.924 1.00 82.05 4733 CA PHE D 506 70.796 103.414 181.227 1.00 74.33 4734 CB PHE D 506 71.026 104.405 180.096 1.00 64.40 4735 CG PHE D 506 71.958 103.925 179.028 1.00 65.82 4736 CD1 PHE D 506 71.821 104.396 177.728 1.00 93.15 4737 CD2 PHE D 506 73.015 103.082 179.321 1.00 97.38 4738 CE1 PHE D 506 72.715 104.046 176.741 1.00 60.40 4739 CE2 PHE D 506 73.920 102.723 178.335 1.00 94.39 4740 CZ PHE D 506 73.770 103.207 177.044 1.00 83.28 4741 C PHE D 506 70.632 104.203 182.525 1.00 84.85 4742 O PHE D 506 69.530 104.648 182.857 1.00 134.54 4743 N SER D 507 71.736 104.387 183.248 1.00 93.21 4744 CA SER D 507 71.722 105.144 184.500 1.00 85.59 4745 CB SER D 507 71.894 104.219 185.700 1.00 41.54 4746 OG SER D 507 71.868 104.985 186.887 1.00 68.49 4747 C SER D 507 72.833 106.187 184.516 1.00 67.47 4748 O SER D 507 73.925 105.945 184.012 1.00 59.51 4749 N ARG D 508 72.550 107.342 185.105 1.00 61.04 4750 CA ARG D 508 73.517 108.428 185.175 1.00 58.84 4751 CB ARG D 508 73.139 109.517 184.167 1.00 49.25 4752 CG ARG D 508 73.977 110.781 184.239 1.00 60.80 4753 CD ARG D 508 73.595 111.707 183.087 1.00 74.40 4754 NE ARG D 508 74.244 113.013 183.150 1.00 57.97 4755 CZ ARG D 508 73.940 113.952 184.042 1.00 108.28 4756 NH1 ARG D 508 72.994 113.730 184.947 1.00 134.73 4757 NH2 ARG D 508 74.574 115.118 184.028 1.00 134.59 4758 C ARG D 508 73.579 108.999 186.586 1.00 66.73 4759 O ARG D 508 72.559 109.381 187.162 1.00 94.10 4760 N LEU D 509 74.792 109.076 187.123 1.00 102.57 4761 CA LEU D 509 75.009 109.556 188.479 1.00 92.49 4762 CB LEU D 509 75.349 108.353 189.361 1.00 65.32 4763 CG LEU D 509 75.820 108.672 190.775 1.00 82.75 4764 CD1 LEU D 509 74.814 109.609 191.434 1.00 121.62 4765 CD2 LEU D 509 75.980 107.383 191.571 1.00 45.98 4766 C LEU D 509 76.108 110.609 188.620 1.00 66.30 4767 O LEU D 509 77.252 110.253 188.843 1.00 62.93 4768 N GLU D 510 75.774 111.893 188.504 1.00 101.58 4769 CA GLU D 510 76.793 112.943 188.641 1.00 93.28 4770 CB GLU D 510 76.143 114.333 188.575 1.00 108.16 4771 CG GLU D 510 75.472 114.649 187.240 1.00 127.89 4772 CD GLU D 510 74.727 115.982 187.233 1.00 158.27 4773 OE1 GLU D 510 73.731 116.114 187.978 1.00 163.67 4774 OE2 GLU D 510 75.133 116.898 186.481 1.00 133.07 4775 C GLU D 510 77.516 112.757 189.981 1.00 107.52 4776 O GLU D 510 76.906 112.303 190.949 1.00 106.06 4777 N VAL D 511 78.808 113.095 190.036 1.00 92.80 4778 CA VAL D 511 79.599 112.937 191.268 1.00 119.85 4779 CB VAL D 511 80.495 111.658 191.193 1.00 42.93 4780 CG1 VAL D 511 81.422 111.579 192.387 1.00 117.40 4781 CG2 VAL D 511 79.622 110.425 191.171 1.00 107.86 4782 C VAL D 511 80.483 114.145 191.640 1.00 159.37 4783 O VAL D 511 80.869 114.943 190.776 1.00 157.18 4784 N THR D 512 80.795 114.261 192.936 1.00 172.76 4785 CA THR D 512 81.622 115.346 193.472 1.00 158.22 4786 CB THR D 512 80.946 116.001 194.700 1.00 168.13 4787 OG1 THR D 512 79.636 116.460 194.340 1.00 167.64 4788 CG2 THR D 512 81.773 117.182 195.203 1.00 185.75 4789 C THR D 512 83.020 114.866 193.889 1.00 141.73 4790 O THR D 512 83.171 113.781 194.468 1.00 95.92 4791 N ARG D 513 84.029 115.691 193.598 1.00 133.96 4792 CA ARG D 513 85.423 115.383 193.919 1.00 137.46 4793 CB ARG D 513 86.296 116.640 193.794 1.00 162.09 4794 CG ARG D 513 87.780 116.393 194.082 1.00 185.62 4795 CD ARG D 513 88.601 117.679 194.049 1.00 208.34 4796 NE ARG D 513 90.013 117.433 194.340 1.00 232.40 4797 CZ ARG D 513 90.943 118.383 194.427 1.00 235.91 4798 NH1 ARG D 513 90.620 119.656 194.244 1.00 230.77 4799 NH2 ARG D 513 92.201 118.059 194.699 1.00 224.77 4800 C ARG D 513 85.580 114.803 195.315 1.00 122.87 4801 O ARG D 513 86.170 113.737 195.499 1.00 77.13 4802 N ALA D 514 85.050 115.520 196.295 1.00 123.66 4803 CA ALA D 514 85.120 115.095 197.682 1.00 119.89 4804 CB ALA D 514 84.105 115.872 198.496 1.00 121.33 4805 C ALA D 514 84.881 113.594 197.847 1.00 114.46 4806 O ALA D 514 85.618 112.909 198.559 1.00 115.15 4807 N GLU D 515 83.860 113.086 197.165 1.00 114.63 4808 CA GLU D 515 83.502 111.677 197.265 1.00 110.01 4809 CB GLU D 515 82.120 111.454 196.648 1.00 77.08 4810 CG GLU D 515 81.013 112.106 197.450 1.00 144.14 4811 CD GLU D 515 79.656 111.961 196.806 1.00 162.03 4812 OE1 GLU D 515 79.475 112.477 195.680 1.00 133.35 4813 OE2 GLU D 515 78.773 111.334 197.431 1.00 167.09 4814 C GLU D 515 84.480 110.641 196.718 1.00 110.50 4815 O GLU D 515 84.593 109.548 197.282 1.00 87.75 4816 N TRP D 516 85.188 110.948 195.635 1.00 88.87 4817 CA TRP D 516 86.111 109.943 195.117 1.00 96.30 4818 CB TRP D 516 86.285 110.065 193.596 1.00 116.50 4819 CG TRP D 516 87.195 111.132 193.088 1.00 89.33 4820 CD2 TRP D 516 86.815 112.276 192.315 1.00 84.44 4821 CE2 TRP D 516 88.002 112.945 191.949 1.00 97.81 4822 CE3 TRP D 516 85.585 112.796 191.892 1.00 94.14 4823 CD1 TRP D 516 88.556 111.159 193.168 1.00 124.94 4824 NE1 TRP D 516 89.050 112.243 192.483 1.00 140.17 4825 CZ2 TRP D 516 87.996 114.115 191.178 1.00 128.17 4826 CZ3 TRP D 516 85.578 113.960 191.125 1.00 81.83 4827 CH2 TRP D 516 86.779 114.604 190.775 1.00 116.38 4828 C TRP D 516 87.452 109.954 195.824 1.00 127.96 4829 O TRP D 516 88.268 109.049 195.640 1.00 148.49 4830 N GLU D 517 87.676 110.982 196.636 1.00 129.08 4831 CA GLU D 517 88.906 111.068 197.400 1.00 111.06 4832 CB GLU D 517 89.239 112.523 197.722 1.00 135.30 4833 CG GLU D 517 89.577 113.349 196.490 1.00 155.78 4834 CD GLU D 517 90.194 114.688 196.834 1.00 196.31 4835 OE1 GLU D 517 89.548 115.475 197.559 1.00 211.98 4836 OE2 GLU D 517 91.328 114.952 196.380 1.00 180.61 4837 C GLU D 517 88.632 110.271 198.668 1.00 124.76 4838 O GLU D 517 89.549 109.710 199.278 1.00 141.89 4839 N GLN D 518 87.352 110.217 199.041 1.00 103.46 4840 CA GLN D 518 86.906 109.467 200.211 1.00 115.30 4841 CB GLN D 518 85.419 109.731 200.463 1.00 143.81 4842 CG GLN D 518 84.866 109.115 201.744 1.00 176.95 4843 CD GLN D 518 83.365 109.327 201.897 1.00 168.05 4844 OE1 GLN D 518 82.879 110.461 201.875 1.00 121.65 4845 NE2 GLN D 518 82.624 108.233 202.053 1.00 146.22 4846 C GLN D 518 87.136 107.988 199.890 1.00 126.60 4847 O GLN D 518 87.433 107.182 200.778 1.00 97.98 4848 N LYS D 519 86.987 107.660 198.605 1.00 133.48 4849 CA LYS D 519 87.195 106.314 198.065 1.00 130.66 4850 CB LYS D 519 86.243 105.295 198.698 1.00 75.97 4851 CG LYS D 519 86.644 103.852 198.402 1.00 89.89 4852 CD LYS D 519 86.097 102.873 199.431 1.00 118.90 4853 CE LYS D 519 86.781 101.513 199.312 1.00 120.25 4854 NZ LYS D 519 86.331 100.555 200.365 1.00 142.07 4855 C LYS D 519 86.960 106.353 196.560 1.00 122.50 4856 O LYS D 519 86.313 107.271 196.063 1.00 112.56 4857 N ASP D 520 87.494 105.364 195.840 1.00 147.72 4858 CA ASP D 520 87.334 105.277 194.383 1.00 101.05 4859 CB ASP D 520 88.642 104.843 193.718 1.00 139.44 4860 CG ASP D 520 89.593 105.997 193.499 1.00 177.33 4861 OD1 ASP D 520 89.228 106.917 192.737 1.00 157.39 4862 OD2 ASP D 520 90.698 105.982 194.086 1.00 181.89 4863 C ASP D 520 86.240 104.292 193.999 1.00 90.40 4864 O ASP D 520 85.540 104.494 193.015 1.00 100.30 4865 N GLU D 521 86.104 103.225 194.783 1.00 113.97 4866 CA GLU D 521 85.096 102.196 194.535 1.00 100.63 4867 CB GLU D 521 85.165 101.093 195.599 1.00 137.88 4868 CG GLU D 521 85.922 99.836 195.206 1.00 152.59 4869 CD GLU D 521 85.646 98.680 196.162 1.00 162.69 4870 OE1 GLU D 521 84.480 98.228 196.228 1.00 124.80 4871 OE2 GLU D 521 86.587 98.228 196.850 1.00 167.89 4872 C GLU D 521 83.661 102.715 194.504 1.00 98.08 4873 O GLU D 521 83.099 103.086 195.534 1.00 104.25 4874 N PHE D 522 83.078 102.726 193.312 1.00 127.92 4875 CA PHE D 522 81.692 103.137 193.112 1.00 85.49 4876 CB PHE D 522 81.596 104.278 192.104 1.00 55.87 4877 CG PHE D 522 81.809 105.627 192.700 1.00 92.01 4878 CD1 PHE D 522 82.876 105.862 193.553 1.00 109.83 4879 CD2 PHE D 522 80.950 106.672 192.392 1.00 125.42 4880 CE1 PHE D 522 83.080 107.123 194.087 1.00 147.56 4881 CE2 PHE D 522 81.146 107.935 192.919 1.00 81.53 4882 CZ PHE D 522 82.208 108.163 193.765 1.00 99.48 4883 C PHE D 522 80.989 101.915 192.556 1.00 91.67 4884 O PHE D 522 81.450 101.315 191.587 1.00 86.92 4885 N ILE D 523 79.879 101.532 193.159 1.00 58.82 4886 CA ILE D 523 79.199 100.360 192.670 1.00 96.62 4887 CB ILE D 523 79.059 99.315 193.791 1.00 67.53 4888 CG2 ILE D 523 78.386 98.043 193.261 1.00 71.95 4889 CG1 ILE D 523 80.448 98.994 194.353 1.00 74.60 4890 CD1 ILE D 523 80.448 97.914 195.426 1.00 142.45 4891 C ILE D 523 77.839 100.700 192.098 1.00 86.74 4892 O ILE D 523 77.110 101.506 192.654 1.00 100.77 4893 N CYS D 524 77.521 100.095 190.961 1.00 98.48 4894 CA CYS D 524 76.236 100.283 190.304 1.00 85.44 4895 C CYS D 524 75.553 98.922 190.326 1.00 64.47 4896 O CYS D 524 75.712 98.128 189.406 1.00 68.44 4897 CB CYS D 524 76.425 100.739 188.861 1.00 71.53 4898 SG CYS D 524 74.938 100.516 187.836 1.00 110.38 4899 N ARG D 525 74.809 98.655 191.395 1.00 92.59 4900 CA ARG D 525 74.107 97.387 191.569 1.00 59.38 4901 CB ARG D 525 73.679 97.234 193.029 1.00 53.65 4902 CG ARG D 525 73.283 95.825 193.416 1.00 62.42 4903 CD ARG D 525 73.547 95.533 194.901 1.00 81.91 4904 NE ARG D 525 72.599 96.177 195.808 1.00 90.24 4905 CZ ARG D 525 72.458 95.846 197.088 1.00 147.65 4906 NH1 ARG D 525 73.206 94.878 197.608 1.00 136.10 4907 NH2 ARG D 525 71.568 96.475 197.847 1.00 130.51 4908 C ARG D 525 72.890 97.286 190.665 1.00 81.55 4909 O ARG D 525 72.477 98.264 190.048 1.00 81.39 4910 N ALA D 526 72.325 96.089 190.590 1.00 78.78 4911 CA ALA D 526 71.152 95.837 189.770 1.00 57.14 4912 CB ALA D 526 71.564 95.534 188.356 1.00 39.11 4913 C ALA D 526 70.393 94.661 190.359 1.00 60.25 4914 O ALA D 526 70.982 93.665 190.776 1.00 67.91 4915 N VAL D 527 69.078 94.783 190.403 1.00 45.78 4916 CA VAL D 527 68.265 93.721 190.958 1.00 62.42 4917 CB VAL D 527 67.445 94.234 192.147 1.00 81.54 4918 CG1 VAL D 527 66.648 93.095 192.766 1.00 72.43 4919 CG2 VAL D 527 68.373 94.871 193.163 1.00 71.57 4920 C VAL D 527 67.326 93.199 189.894 1.00 54.64 4921 O VAL D 527 66.520 93.949 189.356 1.00 97.00 4922 N HIS D 528 67.443 91.914 189.584 1.00 64.63 4923 CA HIS D 528 66.588 91.301 188.581 1.00 51.86 4924 CB HIS D 528 67.337 91.112 187.275 1.00 37.99 4925 CG HIS D 528 66.459 90.762 186.118 1.00 60.26 4926 CD2 HIS D 528 65.631 89.713 185.908 1.00 94.26 4927 ND1 HIS D 528 66.402 91.528 184.973 1.00 110.60 4928 CE1 HIS D 528 65.580 90.963 184.107 1.00 110.22 4929 NE2 HIS D 528 65.099 89.860 184.651 1.00 125.81 4930 C HIS D 528 66.106 89.963 189.080 1.00 60.71 4931 O HIS D 528 66.741 89.363 189.953 1.00 64.08 4932 N GLU D 529 64.979 89.512 188.533 1.00 75.37 4933 CA GLU D 529 64.388 88.250 188.933 1.00 104.01 4934 CB GLU D 529 63.007 88.110 188.318 1.00 133.95 4935 CG GLU D 529 62.316 86.852 188.709 1.00 183.70 4936 CD GLU D 529 60.964 86.726 188.018 1.00 202.90 4937 OE1 GLU D 529 60.677 87.124 186.972 1.00 204.87 4938 OE2 GLU D 529 59.987 86.193 188.379 1.00 194.88 4939 C GLU D 529 65.266 87.069 188.541 1.00 117.67 4940 O GLU D 529 65.146 85.986 189.117 1.00 105.24 4941 N ALA D 530 66.198 87.305 187.616 1.00 104.62 4942 CA ALA D 530 67.094 86.252 187.128 1.00 119.79 4943 CB ALA D 530 67.429 86.491 185.653 1.00 110.35 4944 C ALA D 530 68.381 86.118 187.923 1.00 142.01 4945 O ALA D 530 68.445 85.370 188.898 1.00 165.83 4946 N ALA D 531 69.398 86.844 187.473 1.00 133.84 4947 CA ALA D 531 70.724 86.868 188.083 1.00 167.12 4948 CB ALA D 531 71.135 88.308 188.325 1.00 130.57 4949 C ALA D 531 70.905 86.066 189.370 1.00 184.40 4950 O ALA D 531 70.099 86.152 190.298 1.00 180.48 4951 N SER D 532 71.985 85.294 189.421 1.00 188.26 4952 CA SER D 532 72.294 84.494 190.596 1.00 165.83 4953 CB SER D 532 72.587 83.041 190.197 1.00 154.95 4954 OG SER D 532 71.402 82.364 189.812 1.00 130.00 4955 C SER D 532 73.494 85.093 191.329 1.00 145.61 4956 O SER D 532 74.236 85.909 190.775 1.00 131.77 4957 N PRO D 533 73.700 84.687 192.588 1.00 134.93 4958 CD PRO D 533 74.977 84.898 193.295 1.00 147.80 4959 CA PRO D 533 72.863 83.723 193.308 1.00 118.05 4960 CB PRO D 533 73.891 82.890 194.044 1.00 151.25 4961 CG PRO D 533 74.856 83.964 194.501 1.00 159.03 4962 C PRO D 533 71.913 84.426 194.272 1.00 133.53 4963 O PRO D 533 70.971 83.824 194.796 1.00 89.86 4964 N SER D 534 72.180 85.709 194.496 1.00 145.54 4965 CA SER D 534 71.391 86.530 195.406 1.00 131.75 4966 CB SER D 534 72.330 87.327 196.311 1.00 161.36 4967 OG SER D 534 73.274 88.055 195.538 1.00 169.84 4968 C SER D 534 70.454 87.488 194.679 1.00 120.79 4969 O SER D 534 70.006 88.477 195.250 1.00 109.78 4970 N GLN D 535 70.162 87.192 193.419 1.00 127.46 4971 CA GLN D 535 69.280 88.032 192.618 1.00 106.83 4972 CB GLN D 535 67.887 88.057 193.244 1.00 30.80 4973 CG GLN D 535 67.263 86.683 193.338 1.00 63.61 4974 CD GLN D 535 66.841 86.320 194.746 1.00 103.06 4975 OE1 GLN D 535 67.579 86.550 195.703 1.00 120.06 4976 NE2 GLN D 535 65.654 85.735 194.881 1.00 119.16 4977 C GLN D 535 69.834 89.450 192.454 1.00 81.50 4978 O GLN D 535 69.127 90.369 192.039 1.00 62.58 4979 N THR D 536 71.117 89.603 192.769 1.00 77.55 4980 CA THR D 536 71.818 90.876 192.651 1.00 78.91 4981 CB THR D 536 72.502 91.241 193.964 1.00 101.54 4982 OG1 THR D 536 71.513 91.416 194.980 1.00 139.48 4983 CG2 THR D 536 73.313 92.511 193.812 1.00 91.85 4984 C THR D 536 72.908 90.769 191.583 1.00 88.04 4985 O THR D 536 73.332 89.672 191.225 1.00 115.17 4986 N VAL D 537 73.368 91.914 191.092 1.00 73.07 4987 CA VAL D 537 74.415 91.965 190.078 1.00 83.98 4988 CB VAL D 537 73.851 91.681 188.687 1.00 56.48 4989 CG1 VAL D 537 74.764 92.252 187.629 1.00 76.12 4990 CG2 VAL D 537 73.701 90.191 188.490 1.00 116.74 4991 C VAL D 537 75.041 93.348 190.075 1.00 97.13 4992 O VAL D 537 74.349 94.346 189.894 1.00 104.54 4993 N GLN D 538 76.350 93.415 190.263 1.00 95.87 4994 CA GLN D 538 77.004 94.713 190.296 1.00 90.43 4995 CB GLN D 538 77.204 95.139 191.756 1.00 92.33 4996 CG GLN D 538 77.904 94.094 192.622 1.00 78.35 4997 CD GLN D 538 77.775 94.382 194.105 1.00 103.51 4998 OE1 GLN D 538 76.736 94.108 194.715 1.00 86.43 4999 NE2 GLN D 538 78.829 94.950 194.695 1.00 114.86 5000 C GLN D 538 78.329 94.733 189.554 1.00 78.31 5001 O GLN D 538 78.903 93.684 189.271 1.00 92.93 5002 N ARG D 539 78.794 95.936 189.229 1.00 52.71 5003 CA ARG D 539 80.060 96.120 188.539 1.00 93.72 5004 CB ARG D 539 79.846 96.340 187.042 1.00 98.94 5005 CG ARG D 539 81.128 96.234 186.207 1.00 143.16 5006 CD ARG D 539 81.220 94.892 185.479 1.00 155.59 5007 NE ARG D 539 80.795 93.779 186.324 1.00 160.22 5008 CZ ARG D 539 80.719 92.516 185.921 1.00 144.73 5009 NH1 ARG D 539 81.046 92.195 184.678 1.00 164.97 5010 NH2 ARG D 539 80.302 91.578 186.760 1.00 105.83 5011 C ARG D 539 80.713 97.352 189.131 1.00 116.29 5012 O ARG D 539 80.119 98.424 189.130 1.00 77.60 5013 N ALA D 540 81.933 97.195 189.634 1.00 123.66 5014 CA ALA D 540 82.664 98.303 190.232 1.00 90.79 5015 CB ALA D 540 83.843 97.768 191.030 1.00 120.12 5016 C ALA D 540 83.155 99.291 189.179 1.00 83.01 5017 O ALA D 540 83.133 99.004 187.988 1.00 116.07 5018 N VAL D 541 83.596 100.459 189.629 1.00 73.02 5019 CA VAL D 541 84.107 101.491 188.735 1.00 89.93 5020 CB VAL D 541 82.963 102.295 188.111 1.00 88.65 5021 CG1 VAL D 541 82.228 103.037 189.197 1.00 84.77 5022 CG2 VAL D 541 83.498 103.274 187.069 1.00 53.86 5023 C VAL D 541 84.979 102.443 189.547 1.00 102.56 5024 O VAL D 541 85.129 102.267 190.755 1.00 153.42 5025 N SER D 542 85.550 103.446 188.882 1.00 109.91 5026 CA SER D 542 86.397 104.444 189.533 1.00 97.55 5027 CB SER D 542 87.392 103.773 190.490 1.00 113.18 5028 OG SER D 542 88.174 102.799 189.819 1.00 118.66 5029 C SER D 542 87.169 105.273 188.516 1.00 76.47 5030 O SER D 542 87.411 104.831 187.395 1.00 131.73 5031 N VAL D 543 87.548 106.481 188.909 1.00 61.96 5032 CA VAL D 543 88.325 107.348 188.034 1.00 111.23 5033 CB VAL D 543 88.073 108.846 188.322 1.00 129.59 5034 CG1 VAL D 543 88.348 109.653 187.057 1.00 63.37 5035 CG2 VAL D 543 86.642 109.072 188.868 1.00 29.47 5036 C VAL D 543 89.805 107.068 188.309 1.00 152.73 5037 O VAL D 543 90.167 106.634 189.406 1.00 171.72 5038 N ASN D 544 90.655 107.326 187.320 1.00 149.81 5039 CA ASN D 544 92.091 107.096 187.461 1.00 158.60 5040 CB ASN D 544 92.644 107.880 188.658 1.00 160.72 5041 CG ASN D 544 92.354 109.369 188.568 1.00 151.01 5042 OD1 ASN D 544 92.701 110.027 187.586 1.00 153.71 5043 ND2 ASN D 544 91.716 109.907 189.600 1.00 105.81 5044 C ASN D 544 92.415 105.605 187.627 1.00 162.71 5045 O ASN D 544 93.206 105.090 186.810 1.00 168.57 5046 OXT ASN D 544 91.886 104.965 188.563 1.00 91.11 5047 C1 NAG D 694 45.181 116.572 187.768 1.00 63.34 5048 C2 NAG D 694 45.182 115.814 186.435 1.00 51.52 5049 N2 NAG D 694 43.887 115.931 185.794 1.00 71.95 5050 C7 NAG D 694 43.803 116.134 184.485 1.00 76.86 5051 O7 NAG D 694 43.995 115.243 183.656 1.00 109.89 5052 C8 NAG D 694 43.455 117.540 184.026 1.00 79.33 5053 C3 NAG D 694 45.516 114.334 186.657 1.00 53.42 5054 O3 NAG D 694 45.596 113.666 185.403 1.00 84.81 5055 C4 NAG D 694 46.845 114.203 187.408 1.00 72.20 5056 O4 NAG D 694 47.134 112.810 187.695 1.00 113.39 5057 C5 NAG D 694 46.776 115.015 188.712 1.00 81.05 5058 O5 NAG D 694 46.445 116.403 188.432 1.00 76.78 5059 C6 NAG D 694 48.102 115.016 189.457 1.00 135.14 5060 O6 NAG D 694 49.101 115.734 188.742 1.00 168.86 5061 C1 NAG D 695 48.197 112.221 187.004 1.00 162.56 5062 C2 NAG D 695 49.047 111.359 187.959 1.00 161.99 5063 N2 NAG D 695 49.643 112.180 188.999 1.00 176.87 5064 C7 NAG D 695 49.835 111.675 190.216 1.00 158.22 5065 O7 NAG D 695 50.822 111.000 190.511 1.00 158.06 5066 C8 NAG D 695 48.769 111.953 191.265 1.00 108.38 5067 C3 NAG D 695 50.146 110.631 187.168 1.00 149.27 5068 O3 NAG D 695 50.894 109.785 188.028 1.00 157.06 5069 C4 NAG D 695 49.521 109.804 186.043 1.00 139.32 5070 O4 NAG D 695 50.565 109.173 185.262 1.00 134.98 5071 C5 NAG D 695 48.678 110.741 185.160 1.00 171.70 5072 O5 NAG D 695 47.654 111.397 185.953 1.00 147.36 5073 C6 NAG D 695 47.969 110.032 184.022 1.00 163.04 5074 O6 NAG D 695 47.105 110.920 183.327 1.00 154.34 5075 C1 MAN D 696 50.684 107.790 185.360 1.00 151.20 5076 C2 MAN D 696 51.539 107.258 184.202 1.00 196.02 5077 O2 MAN D 696 52.807 107.901 184.205 1.00 199.76 5078 C3 MAN D 696 51.725 105.743 184.350 1.00 186.47 5079 O3 MAN D 696 52.588 105.259 183.329 1.00 168.62 5080 C4 MAN D 696 52.308 105.414 185.732 1.00 184.79 5081 O4 MAN D 696 52.356 104.004 185.908 1.00 169.18 5082 C5 MAN D 696 51.437 106.043 186.831 1.00 155.53 5083 O5 MAN D 696 51.309 107.471 186.616 1.00 152.57 5084 C6 MAN D 696 51.972 105.838 188.246 1.00 138.84 5085 O6 MAN D 696 53.387 105.694 188.271 1.00 130.94 5086 C1 CPS E 101 26.312 116.112 182.219 1.00 5.42 5087 C2 CPS E 101 25.430 116.494 183.392 1.00 42.91 5088 C3 CPS E 101 25.569 114.197 184.531 1.00 20.32 5089 C4 CPS E 101 25.066 112.803 185.246 1.00 43.57 5090 C5 CPS E 101 24.092 113.131 186.307 1.00 40.19 5091 C6 CPS E 101 23.154 114.241 185.856 1.00 48.37 5092 C7 CPS E 101 22.219 114.521 186.964 1.00 35.77 5093 C8 CPS E 101 22.186 113.112 187.776 1.00 46.50 5094 C9 CPS E 101 23.212 112.183 186.927 1.00 21.17 5095 C10 CPS E 101 25.033 113.895 187.520 1.00 6.18 5096 C11 CPS E 101 26.201 117.156 184.612 1.00 11.25 5097 C12 CPS E 101 25.595 115.700 180.948 1.00 105.46 5098 C13 CPS E 101 24.630 116.690 180.447 1.00 51.23 5099 C14 CPS E 101 23.589 117.028 181.573 1.00 47.83 5100 C15 CPS E 101 24.383 117.491 182.865 1.00 15.76 5101 C16 CPS E 101 23.421 117.851 183.910 1.00 38.47 5102 C17 CPS E 101 22.681 116.741 184.654 1.00 63.19 5103 C18 CPS E 101 23.637 115.556 185.273 1.00 9.51 5104 C19 CPS E 101 24.660 115.277 183.985 1.00 10.09 5105 C20 CPS E 101 23.634 111.029 187.910 1.00 16.56 5106 C21 CPS E 101 24.712 110.080 187.465 1.00 66.60 5107 C22 CPS E 101 22.307 110.241 188.314 1.00 66.32 5108 C23 CPS E 101 22.401 109.119 189.237 1.00 40.09 5109 O2 CPS E 101 23.891 116.247 179.167 1.00 70.91 5110 O3 CPS E 101 21.848 116.073 183.892 1.00 56.49 5111 O4 CPS E 101 24.411 112.252 184.392 1.00 89.45 5112 C1 CHA E 102 30.416 120.373 183.529 1.00 52.35 5113 C2 CHA E 102 29.113 120.721 182.838 1.00 60.47 5114 C3 CHA E 102 29.802 119.956 180.443 1.00 57.28 5115 C4 CHA E 102 30.034 120.057 178.819 1.00 61.04 5116 C5 CHA E 102 28.820 120.636 178.155 1.00 63.59 5117 C6 CHA E 102 28.187 121.729 178.965 1.00 68.16 5118 C7 CHA E 102 26.964 122.165 178.185 1.00 71.21 5119 C8 CHA E 102 27.365 121.780 176.626 1.00 72.34 5120 C9 CHA E 102 28.850 121.169 176.840 1.00 68.39 5121 C10 CHA E 102 27.634 119.363 178.205 1.00 37.85 5122 C11 CHA E 102 28.076 119.543 182.924 1.00 58.04 5123 C12 CHA E 102 31.426 121.484 183.528 1.00 61.79 5124 C13 CHA E 102 30.933 122.729 184.176 1.00 64.51 5125 C14 CHA E 102 29.611 123.203 183.499 1.00 70.75 5126 C15 CHA E 102 28.577 121.993 183.504 1.00 67.54 5127 C16 CHA E 102 27.325 122.461 182.894 1.00 75.83 5128 C17 CHA E 102 27.241 122.710 181.390 1.00 74.20 5129 C18 CHA E 102 27.880 121.531 180.440 1.00 63.18 5130 C19 CHA E 102 29.262 121.064 181.304 1.00 59.69 5131 C20 CHA E 102 29.225 120.329 175.558 1.00 70.63 5132 C21 CHA E 102 30.563 119.632 175.630 1.00 85.68 5133 C22 CHA E 102 29.152 121.269 174.231 1.00 65.66 5134 C23 CHA E 102 29.532 120.583 172.993 1.00 60.28 5135 O2 CHA E 102 31.918 123.917 184.175 1.00 72.67 5136 O3 CHA E 102 27.885 123.807 181.001 1.00 76.62 5137 O4 CHA E 102 30.868 120.933 178.735 1.00 61.67 5138 C24 CHA E 102 30.917 120.626 172.750 1.00 70.84 5139 O5 CHA E 102 31.747 121.244 173.427 1.00 86.94 5140 N25 CHA E 102 31.345 119.924 171.722 1.00 71.63 5141 C25 CHA E 102 35.585 118.656 169.928 1.00 97.77 5142 C26 CHA E 102 37.184 119.547 171.582 1.00 101.45 5143 C27 CHA E 102 32.967 119.825 171.396 1.00 81.57 5144 C28 CHA E 102 33.756 119.017 172.519 1.00 73.52 5145 C29 CHA E 102 35.099 118.469 172.437 1.00 83.76 5146 N1 CHA E 102 36.183 118.470 171.311 1.00 101.30 5147 C30 CHA E 102 36.851 117.076 171.401 1.00 103.79 5148 C31 CHA E 102 37.861 116.562 172.339 1.00 103.99 5149 C32 CHA E 102 38.216 115.072 172.105 1.00 101.66 5150 S1 CHA E 102 37.044 114.052 172.308 1.00 98.10 5151 O6 CHA E 102 37.726 112.791 172.029 1.00 94.90 5152 O7 CHA E 102 36.530 114.113 173.536 1.00 94.04 5153 O8 CHA E 102 36.102 114.281 171.234 1.00 98.37 5154 C1 CPS E 103 32.216 113.269 184.109 1.00 78.09 5155 C2 CPS E 103 30.907 113.504 184.849 1.00 57.43 5156 C3 CPS E 103 31.645 115.680 185.963 1.00 11.62 5157 C4 CPS E 103 31.940 116.766 187.130 1.00 85.58 5158 C5 CPS E 103 30.773 116.851 188.064 1.00 75.94 5159 C6 CPS E 103 30.148 115.491 188.287 1.00 54.40 5160 C7 CPS E 103 29.007 115.648 189.227 1.00 38.04 5161 C8 CPS E 103 29.435 116.990 190.053 1.00 99.76 5162 C9 CPS E 103 30.861 117.406 189.365 1.00 99.01 5163 C10 CPS E 103 29.523 117.654 187.165 1.00 26.64 5164 C11 CPS E 103 29.830 114.271 183.974 1.00 86.48 5165 C12 CPS E 103 33.215 112.383 184.837 1.00 41.22 5166 C13 CPS E 103 32.685 111.063 185.227 1.00 35.35 5167 C14 CPS E 103 31.396 111.225 186.094 1.00 60.04 5168 C15 CPS E 103 30.372 112.125 185.283 1.00 60.63 5169 C16 CPS E 103 29.149 112.239 186.070 1.00 26.81 5170 C17 CPS E 103 29.099 113.110 187.300 1.00 68.24 5171 C18 CPS E 103 29.746 114.600 187.134 1.00 25.03 5172 C19 CPS E 103 31.088 114.294 186.172 1.00 47.93 5173 C20 CPS E 103 31.120 118.945 189.692 1.00 143.80 5174 C21 CPS E 103 32.295 119.650 189.055 1.00 182.24 5175 C22 CPS E 103 31.182 119.088 191.263 1.00 162.60 5176 C23 CPS E 103 31.415 120.407 191.794 1.00 169.03 5177 O2 CPS E 103 33.678 110.186 185.988 1.00 96.90 5178 O3 CPS E 103 29.754 112.603 188.293 1.00 39.74 5179 O4 CPS E 103 32.821 116.237 187.761 1.00 105.48 5180 C1 CPS E 104 20.969 119.198 190.086 1.00 129.45 5181 C2 CPS E 104 21.575 119.457 188.703 1.00 48.78 5182 C3 CPS E 104 23.879 120.110 189.583 1.00 31.80 5183 C4 CPS E 104 25.238 120.987 189.816 1.00 107.94 5184 C5 CPS E 104 25.780 121.443 188.506 1.00 77.04 5185 C6 CPS E 104 24.660 121.867 187.572 1.00 43.50 5186 C7 CPS E 104 25.269 122.326 186.286 1.00 45.84 5187 C8 CPS E 104 26.760 122.793 186.764 1.00 97.93 5188 C9 CPS E 104 26.767 122.465 188.375 1.00 99.02 5189 C10 CPS E 104 26.370 119.995 187.748 1.00 36.89 5190 C11 CPS E 104 22.163 118.151 188.039 1.00 55.12 5191 C12 CPS E 104 20.228 120.384 190.698 1.00 194.25 5192 C13 CPS E 104 19.160 120.964 189.834 1.00 176.18 5193 C14 CPS E 104 19.732 121.345 188.421 1.00 77.57 5194 C15 CPS E 104 20.460 120.068 187.809 1.00 66.30 5195 C16 CPS E 104 20.958 120.428 186.479 1.00 100.76 5196 C17 CPS E 104 22.157 121.368 186.362 1.00 79.09 5197 C18 CPS E 104 23.461 120.969 187.291 1.00 12.31 5198 C19 CPS E 104 22.712 120.523 188.734 1.00 52.66 5199 C20 CPS E 104 28.295 122.305 188.812 1.00 102.44 5200 C21 CPS E 104 28.602 121.819 190.202 1.00 40.31 5201 C22 CPS E 104 29.033 123.678 188.532 1.00 97.92 5202 C23 CPS E 104 30.441 123.753 188.854 1.00 59.31 5203 O2 CPS E 104 18.441 122.194 190.434 1.00 131.97 5204 O3 CPS E 104 21.885 122.594 186.735 1.00 102.52 5205 O4 CPS E 104 24.841 121.994 190.360 1.00 113.49 5206 C1 CPS E 105 23.987 110.282 194.190 1.00 124.07 5207 C2 CPS E 105 23.504 111.201 193.051 1.00 179.02 5208 C3 CPS E 105 25.048 113.150 193.677 1.00 146.55 5209 C4 CPS E 105 25.528 114.656 194.049 1.00 150.36 5210 C5 CPS E 105 24.986 115.634 193.073 1.00 150.31 5211 C6 CPS E 105 23.542 115.307 192.719 1.00 151.98 5212 C7 CPS E 105 23.086 116.345 191.744 1.00 129.40 5213 C8 CPS E 105 24.069 117.613 192.103 1.00 138.46 5214 C9 CPS E 105 25.016 117.025 193.307 1.00 158.19 5215 C10 CPS E 105 25.809 115.351 191.555 1.00 57.99 5216 C11 CPS E 105 24.253 110.935 191.681 1.00 168.46 5217 C12 CPS E 105 23.199 110.388 195.482 1.00 171.52 5218 C13 CPS E 105 21.738 110.182 195.325 1.00 189.12 5219 C14 CPS E 105 21.142 111.149 194.226 1.00 180.63 5220 C15 CPS E 105 21.981 110.976 192.870 1.00 180.59 5221 C16 CPS E 105 21.395 111.864 191.831 1.00 152.08 5222 C17 CPS E 105 21.590 113.385 191.907 1.00 149.04 5223 C18 CPS E 105 23.124 113.895 192.254 1.00 131.84 5224 C19 CPS E 105 23.632 112.728 193.398 1.00 173.79 5225 C20 CPS E 105 26.373 117.881 193.364 1.00 141.17 5226 C21 CPS E 105 27.491 117.441 194.289 1.00 61.94 5227 C22 CPS E 105 26.007 119.377 193.665 1.00 163.34 5228 C23 CPS E 105 27.114 120.298 193.745 1.00 162.44 5229 O2 CPS E 105 20.934 110.337 196.634 1.00 146.47 5230 O3 CPS E 105 20.861 113.951 192.840 1.00 182.07 5231 O4 CPS E 105 24.940 114.899 195.082 1.00 183.30 5232 S SO4 F 101 26.461 117.594 160.481 1.00 117.04 5233 O1 SO4 F 101 26.028 117.364 161.888 1.00 114.89 5234 O2 SO4 F 101 25.645 118.674 159.871 1.00 116.85 5235 O3 SO4 F 101 27.889 117.990 160.442 1.00 104.02 5236 O4 SO4 F 101 26.264 116.346 159.701 1.00 116.98 5237 S SO4 F 102 30.691 115.815 152.464 1.00 84.09 5238 O1 SO4 F 102 31.425 115.760 153.735 1.00 75.95 5239 O2 SO4 F 102 30.165 117.185 152.282 1.00 88.58 5240 O3 SO4 F 102 31.591 115.536 151.339 1.00 88.44 5241 O4 SO4 F 102 29.608 114.799 152.483 1.00 82.42 5242 S SO4 F 103 21.641 101.569 151.307 1.00 92.25 5243 O1 SO4 F 103 22.530 100.415 151.659 1.00 115.82 5244 O2 SO4 F 103 21.490 102.482 152.472 1.00 115.45 5245 O3 SO4 F 103 22.255 102.282 150.149 1.00 112.57 5246 O4 SO4 F 103 20.304 101.049 150.949 1.00 111.09 5247 S SO4 F 104 63.588 107.320 177.755 1.00 90.55 5248 O1 SO4 F 104 64.167 105.957 177.946 1.00 104.42 5249 O2 SO4 F 104 63.018 107.748 179.075 1.00 101.96 5250 O3 SO4 F 104 64.623 108.285 177.316 1.00 107.44 5251 O4 SO4 F 104 62.568 107.276 176.668 1.00 101.74 5252 S SO4 F 105 38.290 100.112 181.573 1.00 94.13 5253 O1 SO4 F 105 39.110 99.271 182.495 1.00 100.20 5254 O2 SO4 F 105 36.859 99.943 181.952 1.00 108.28 5255 O3 SO4 F 105 38.642 101.562 181.681 1.00 98.51 5256 O4 SO4 F 105 38.529 99.646 180.172 1.00 109.17

[0035] As used herein, an atomic coordinate, also referred to herein as a structure coordinate or coordinate, is a mathematical coordinate derived from mathematical equations related to the patterns obtained on diffraction of X-rays by the atoms of a protein or complex crystal. The diffraction data are typically used to calculate an electron density map, such as that shown in FIG. 1, which is used to establish the positions of the individual atoms within the unit cell of the crystal. A model that substantially represents the atomic coordinates specified in Table 1 includes not only models that literally represent the coordinates but also models representing a coordinate transformation of such atomic coordinates, for example, by changing the spatial orientation of the coordinates.

[0036] The present invention also includes a 3-D model that is a modification of a 3-D model that substantially represents the atomic coordinates specified in Table 1. As used herein, a modification, also referred to herein as a model modification, is a model that represents a complex between a protein that binds to a Fc domain of an antibody and an antibody Fc regon that binds to a Fc receptor protein. A model modification includes, but is not limited to: a refinement of the model that substantially represents the atomic coordinates specified in Table 1; a model representing a complex between any Fc-binding fragment of a Fc receptor protein and any FcR-binding fragment of an antibody having the atomic coordinates specified in Table 1; a model based on other FcεRIα:Fc-Cε3/Cε4 crystals, such as a model based on one or more of the crystals disclosed in the Examples; a model produced using homology modeling techniques to, for example, incorporate all or any part of the amino acid sequence of another FcR or antibody into a 3-D model substantially representing the atomic coordinates specified in Table 1 or incorporate all or any part of the amino acid sequence of a FcεRIα protein or Fc-Cε3/Cε4 into a 3-D model of a complex between another FcR and antibody; and a modification representing a complex between an FcR and antibody, at least one of which has an altered function, which preferably can be used to design a mutein with an improved function compared to an unmodified protein. As used herein, the term unmodified protein refers to a protein that has not been intentionally subjected to either random or site-directed (i.e., targeted) mutagenesis.

[0037] A model of the present invention can be represented in a variety of forms including, but not limited to, listing the coordinates of all atoms comprising the model, providing a physical 3-D model, imaging the model on a computer screen, providing a picture of said model, and deriving a set of coordinates based of a picture of the model, for example by extracting coordinates from a picture or placing a similar immunoglobulin domain into the 3-D model of a human FcεRIα₁₋₁₇₆ protein having SEQ ID NO:2 and deriving a model of the similar domain. Physical 3-D models are tangible and include, but are not limited to, stick models and space-filling models. The phrase “imaging the model on a computer screen” refers to the ability to express (or represent) and manipulate the model on a computer screen using appropriate computer hardware and software technology known to those skilled in the art. Such technology is available from a variety of sources including, for example, Evans and Sutherland, Salt Lake City, Utah, Biosym Technologies, San Diego, Calif., Tripos, Inc., and Molecular Simulations Inc. The phrase “providing a picture of the model” refers to the ability to generate a “hard copy” of the model. Hard copies include both motion and still pictures. Computer screen images and pictures of the model can be visualized in a number of formats including, but not limited to, electron density maps, ribbon diagrams, space-filling representations, a carbon traces, topology diagrams, lists of interatomic vectors, phi/psi/chi angle representations of the coordinates, and contact maps, examples of some of which are in the Figs. Representations of the model can include the entire model or portions thereof. A model can also be represented in a database.

[0038] A model of the present invention also defines the space surrounding that model. Such a space can be represented as a mold, or alpha-space, that can be used to predict the shape of a compound that inhibits the binding of a FcR and antibody.

[0039] In one embodiment, a model of the present invention identifies the solvent accessibility of amino acid residues of the corresponding proteins in the complex. The solvent accessibilities of the amino acids in the complex between PhFcεRIα_(1-176mut) and PhFc-Cε3/Cε4₁₋₂₂₂ are indicated in Table 2. TABLE 2 com14i_deposit.pdb Residue Exposure Surface plot for: structure file = com14h_gen.mtf coordinate set = com14i.pdb TOTAL ACCESSIBLE AREA segid resid resname residue mainchain sidechain A 1 VAL 187.3253 57.6982 129.6271 A 2 PRO 92.7850 27.8208 64.9642 A 3 GLN 136.0547 22.4120 113.6427 A 4 LYS 115.4501 16.7110 98.7391 A 5 PRO 15.6134 5.2823 10.3310 A 6 LYS 129.5753 2.2724 127.3029 A 7 VAL 13.2508 10.5326 2.7182 A 8 SER 61.2891 6.5958 54.6932 A 9 LEU 29.3720 15.0058 14.3663 A 10 ASN 96.3611 5.4707 90.8904 A 11 PRO 61.5816 1.0093 60.5723 A 12 PRO 44.6585 3.6780 40.9805 A 13 TRP 32.1306 0.0000 32.1306 A 14 ASN 13.9201 0.0000 13.9201 A 15 ARG 18.9379 0.0000 18.9379 A 16 ILE 4.0671 0.0000 4.0671 A 17 PHE 2.5761 0.0015 2.5746 A 18 LYS 75.4097 9.6110 65.7987 A 19 GLY 30.4736 30.4736 0.0000 A 20 GLU 38.0623 1.4738 36.5885 A 21 ASN 44.5154 12.5957 31.9196 A 22 VAL 6.0341 5.5689 0.4652 A 23 THR 30.3454 0.0015 30.3439 A 24 LEU 1.9937 0.0005 1.9933 A 25 TER 45.1783 0.8036 44.3747 A 26 CYS 1.8288 1.8288 0.0000 A 27 ASN 45.5609 16.4355 29.1253 A 28 GLY 57.0567 57.0567 0.0000 A 29 ASN 92.9262 33.7771 59.1490 A 30 ASN 13.5663 9.6698 3.8965 A 31 PHE 164.0905 20.6501 143.4404 A 32 PHE 182.6224 29.9619 152.6604 A 33 GLU 98.9835 23.5598 75.4237 A 34 VAL 112.1392 35.9284 76.2108 A 35 SER 13.8929 11.8212 2.0717 A 36 SER 61.4988 16.1241 45.3747 A 37 THR 3.8229 1.4419 2.3810 A 38 LYS 54.6368 1.5373 53.0995 A 39 TRP 0.7682 0.0026 0.7656 A 40 PHE 35.2234 0.8384 34.3850 A 41 HIS 42.4410 4.2641 38.1769 A 42 ASN 55.8729 34.7289 21.1439 A 43 GLY 50.2523 50.2523 0.0000 A 44 SER 90.0908 14.2647 75.8261 A 45 LEU 112.2293 26.8607 85.3687 A 46 SER 33.6534 12.6061 21.0473 A 47 GLU 173.0167 28.6974 144.3194 A 48 GLU 52.6512 0.9816 51.6696 A 49 THR 78.9495 4.5450 74.4045 A 50 ASN 83.8564 1.8107 82.0457 A 51 SER 20.5641 0.7215 19.8427 A 52 SER 44.0129 2.6102 41.4027 A 53 LEU 23.9390 0.2187 23.7203 A 54 ASN 93.7074 14.6559 79.0515 A 55 ILE 14.9901 7.9277 7.0624 A 56 VAL 77.8026 18.1671 59.6354 A 57 ASN 72.5436 10.8218 61.7218 A 58 ALA 0.1748 0.1748 0.0000 A 59 LYS 78.3995 0.3905 78.0090 A 60 PHE 13.8474 0.0000 13.8474 A 61 GLU 71.1840 0.7867 70.3974 A 62 ASP 37.6798 0.0000 37.6798 A 63 SER 0.7611 0.0000 0.7611 A 64 GLY 10.5710 10.5710 0.0000 A 65 GLU 48.7849 0.8856 47.8993 A 66 TYR 9.3817 0.0000 9.3817 A 67 LYS 39.4871 0.0208 39.4662 A 68 CYS 0.0000 0.0000 0.0000 A 69 GLN 32.8025 0.0000 32.8025 A 70 HIS 28.9440 3.7554 25.1886 A 71 GLN 127.6128 34.5779 93.0349 A 72 GLN 114.7755 18.7035 96.0721 A 73 VAL 129.4891 13.4243 116.0648 A 74 ALA 32.5769 10.0706 22.5064 A 75 GLU 64.6775 8.8568 55.8208 A 76 SER 1.9255 1.8897 0.0358 A 77 GLU 112.0982 4.5586 107.5397 A 78 PRO 50.1437 14.6260 35.5177 A 79 VAL 26.4528 3.6105 22.8422 A 80 TYR 121.0925 5.3004 115.7921 A 81 LEU 1.8512 0.7930 1.0581 A 82 GLU 59.7116 0.0003 59.7113 A 83 VAL 9.5413 9.5413 0.0000 A 84 PHE 35.6448 3.2623 32.3825 A 85 SER 24.8318 9.3417 15.4901 A 86 ASP 22.6050 0.0005 22.6045 A 87 TRP 25.2208 0.6392 24.5816 A 88 LEU 3.0061 3.0061 0.0000 A 89 LEU 4.7629 1.9707 2.7922 A 90 LEU 0.6339 0.6339 0.0000 A 91 GLN 0.7211 0.0000 0.7211 A 92 ALA 1.9224 0.9484 0.9739 A 93 SER 28.3506 16.9666 11.3840 A 94 ALA 31.9213 3.2557 28.6657 A 95 GLU 59.5399 4.5153 55.0246 A 96 VAL 90.3253 19.0678 71.2575 A 97 VAL 6.3340 1.9033 4.4307 A 98 MET 117.6508 1.1378 116.5130 A 99 GLU 87.6346 20.1858 67.4487 A 100 GLY 37.5111 37.5111 0.0000 A 101 GLN 86.3207 1.7512 84.5695 A 102 PRO 60.8738 6.3890 54.4848 A 103 LEU 0.4221 0.0000 0.4221 A 104 PHE 80.0346 0.0026 80.0320 A 105 LEU 0.1253 0.1242 0.0011 A 106 ARG 68.1925 0.0000 68.1925 A 107 CYS 3.4779 3.4779 0.0000 A 108 HIS 11.8995 0.9286 10.9708 A 109 GLY 3.1287 3.1287 0.0000 A 110 TRP 32.3303 0.5358 31.7945 A 111 ARG 102.0115 29.5393 72.4722 A 112 ASN 103.7825 16.7021 87.0804 A 113 TRP 8.0187 5.9544 2.0643 A 114 ASP 56.0982 5.8709 50.2273 A 115 VAL 3.8019 3.8019 0.0000 A 116 TYR 28.0985 0.0025 28.0959 A 117 LYS 13.8640 4.0420 9.8220 A 118 VAL 0.0000 0.0000 0.0000 A 119 ILE 2.9639 0.0000 2.9639 A 120 TYR 0.0664 0.0000 0.0664 A 121 TYR 33.2837 0.0000 33.2837 A 122 LYS 25.5895 0.0240 25.5655 A 123 ASP 78.1271 25.4180 52.7091 A 124 GLY 62.3032 62.3032 0.0000 A 125 GLU 120.1814 5.1946 114.9868 A 126 ALA 31.3601 27.4382 3.9219 A 127 LEU 76.9250 25.4102 51.5147 A 128 LYS 112.4216 4.4777 107.9440 A 129 TYR 5.7182 5.6069 0.1112 A 130 TRP 71.2318 0.0019 71.2299 A 131 TYR 2.3182 1.8150 0.5032 A 132 GLU 48.8765 0.0000 48.8765 A 133 ASN 56.4646 18.4026 38.0620 A 134 HIS 34.7605 14.3500 20.4105 A 135 ALA 61.0033 21.2841 39.7192 A 136 ILE 12.9140 2.0093 10.9047 A 137 SER 71.4379 27.1612 44.2767 A 138 ILE 24.6119 3.4516 21.1603 A 139 THR 103.9450 8.8762 95.0688 A 140 ASN 102.3330 12.7166 89.6164 A 141 ALA 10.3600 10.0810 0.2790 A 142 ALA 34.0280 8.3960 25.6320 A 143 VAL 104.7568 10.1018 94.6550 A 144 GLU 126.9246 18.8779 108.0467 A 145 ASP 16.9194 0.0000 16.9194 A 146 SER 21.5373 4.0635 17.4739 A 147 GLY 5.8021 5.8021 0.0000 A 148 THR 32.5295 0.0829 32.4466 A 149 TYR 0.0642 0.0000 0.0642 A 150 TYR 43.8958 0.0226 43.8733 A 151 CYS 0.0000 0.0000 0.0000 A 152 THR 29.2303 0.0000 29.2303 A 153 GLY 3.9813 3.9813 0.0000 A 154 LYS 48.4892 0.3347 48.1546 A 155 VAL 2.0858 0.5817 1.5040 A 156 TRP 18.7900 7.0495 11.7404 A 157 GLN 31.8404 12.3565 19.4840 A 158 LEU 36.5178 1.3940 35.1238 A 159 ASP 102.6316 23.8299 78.8017 A 160 TYR 48.3992 8.9529 39.4463 A 161 GLU 105.3209 20.1949 85.1260 A 162 SER 3.4294 3.2706 0.1588 A 163 GLU 82.4632 5.8768 76.5864 A 164 PRO 93.8712 16.5130 77.3582 A 165 LEU 14.1332 2.3506 11.7826 A 166 ASN 40.8356 7.7631 33.0724 A 167 ILE 1.0917 1.0901 0.0016 A 168 THR 60.5937 0.4273 60.1664 A 169 VAL 30.1152 27.9591 2.1560 A 170 ILE 90.8904 5.5150 85.3753 A 171 LYS 136.7114 19.0209 117.6905 A 172 ALA 86.7389 24.6924 62.0465 A 173 PRO 192.4729 58.6006 133.8723 A 221 NAG 140.3112 0.0000 140.3112 A 222 NAG 177.5229 0.0000 177.5229 A 223 MAN 225.6042 0.0000 225.6042 A 224 FUC 193.3727 0.0000 193.3727 A 242 NAG 142.0058 0.0000 142.0058 A 243 NAG 139.1866 0.0000 139.1866 A 244 MAN 61.6458 0.0000 61.6458 A 245 MAN 221.3300 0.0000 221.3300 A 246 MAN 162.9047 0.0000 162.9047 A 366 NAG 163.0167 0.0000 163.0167 A 367 NAG 271.0832 0.0000 271.0832 A 369 FUC 170.1425 0.0000 170.1425 B 328 PRO 172.3911 55.4048 116.9864 B 329 CYS 28.4788 7.8618 20.6170 B 330 ASP 92.8612 15.7041 77.1570 B 331 SER 27.0273 1.1252 25.9021 B 332 ASN 34.9448 0.0015 34.9432 B 333 PRO 0.0000 0.0000 0.0000 B 334 ARG 56.1569 7.6844 48.4725 B 335 GLY 1.1847 1.1847 0.0000 B 336 VAL 0.0012 0.0012 0.0000 B 337 SER 15.0140 0.0510 14.9630 B 338 ALA 5.2899 4.7848 0.5050 B 339 TYR 51.0452 3.6676 47.3776 B 340 LEU 29.3001 25.9417 3.3584 B 341 SER 45.2273 8.8444 36.3829 B 342 ARG 88.6974 12.2167 76.4807 B 343 PRO 8.9769 8.9769 0.0000 B 344 SER 38.4813 6.2806 32.2008 B 345 PRO 14.1279 3.1946 10.9334 B 346 PHE 47.7276 0.0000 47.7276 B 347 ASP 47.1591 0.0000 47.1591 B 348 LEU 7.6413 0.3974 7.2439 B 349 PHE 17.8265 8.5197 9.3068 B 350 ILE 46.3116 12.5396 33.7719 B 351 ARG 138.4411 22.8644 115.5766 B 352 LYS 138.7623 15.9014 122.8608 B 353 SER 48.1246 7.3438 40.7808 B 354 PRO 3.8128 1.3726 2.4402 B 355 THR 55.0488 11.3329 43.7158 B 356 ILE 0.4059 0.4059 0.0000 B 357 THR 39.8398 :L.4897 38.3501 B 358 CYS 0.3982 0.0000 0.3982 B 359 LEU 21.2325 0.0000 21.2325 B 360 VAL 0.6920 0.0000 0.6920 B 361 VAL 0.7258 0.0000 0.7258 B 362 ASP 6.8200 0.2493 6.5707 B 363 LEU 4.2335 0.0000 4.2335 B 364 ALA 3.3493 2.6950 0.6543 B 365 PRO 82.6759 12.6105 70.0654 B 366 SER 50.6093 40.2181 10.3912 B 367 LYS 213.9320 43.2881 170.6439 B 368 GLY 40.8947 40.8947 0.0000 B 369 THR 86.8598 19.7007 67.1591 B 370 VAL 15.5137 7.3337 8.1800 B 371 ASN 81.8915 3.4400 78.4515 B 372 LEU 22.8095 18.5551 4.2544 B 373 THR 63.4928 3.2688 60.2240 B 374 TRP 23.4425 13.9341 9.5085 B 375 SER 45.2542 3.8130 41.4412 B 376 ARG 46.0272 18.4454 27.5818 B 377 ALA 72.9508 41.9432 31.0077 B 378 SER 61.4249 42.7807 18.6442 B 379 GLY 62.6791 62.6791 0.0000 B 380 LYS 117.6325 4.9136 112.7189 B 381 PRO 121.4544 18.6968 102.7576 B 382 VAL 56.2720 27.9106 28.3614 B 383 ASN 91.2257 9.8352 81.3905 B 384 HIS 171.4010 14.9519 156.4491 B 385 SER 60.0998 34.1545 25.9453 B 386 THR 61.8510 7.3810 54.4700 B 387 ARG 90.5383 34.3831 56.1553 B 388 LYS 116.7691 6.8649 109.9042 B 389 GLU 68.1229 29.0561 39.0668 B 390 GLU 95.8196 5.5952 90.2244 B 391 LYS 165.8039 23.0467 142.7572 B 392 GLN 28.9793 6.2030 22.7763 B 393 ARG 216.3236 21.7321 194.5916 B 394 ASN 21.4124 2.2263 19.1861 B 395 GLY 18.5421 18.5421 0.0000 B 396 THR 1.4681 0.8446 0.6234 B 397 LEU 27.8812 0.0001 27.8811 B 398 THR 2.5805 0.0070 2.5735 B 399 VAL 0.2989 0.0000 0.2989 B 400 THR 28.7559 0.0010 28.7549 B 401 SER 1.6019 0.0320 1.5699 B 402 THR 38.8714 1.4031 37.4684 B 403 LEU 1.4485 0.0026 1.4459 B 404 PRO 54.7046 5.1244 49.5802 B 405 VAL 9.9534 9.2686 0.6848 B 406 GLY 19.5973 19.5973 0.0000 B 407 THR 17.5422 0.0269 17.5153 B 408 ARG 149.2990 4.0416 145.2574 B 409 ASP 50.9581 6.4926 44.4655 B 410 TRP 13.6629 0.0000 13.6629 B 411 ILE 58.9623 7.5292 51.4331 B 412 GLU 150.4506 36.6377 113.8129 B 413 GLY 37.5912 37.5912 0.0000 B 414 GLU 20.7783 6.9542 13.8241 B 415 THR 41.3262 0.7425 40.5837 B 416 TYR 9.7756 0.0127 9.7629 B 417 GLN 62.7741 0.0234 62.7507 B 418 CYS 0.5661 0.4620 0.1041 B 419 ARG 116.8504 0.4330 116.4174 B 420 VAL 3.0810 0.0024 3.0786 B 421 THR 53.9214 2.2639 51.6575 B 422 HIS 11.9613 3.7559 8.2055 B 423 PRO 118.2970 36.7814 81.5157 B 424 HIS 41.1729 9.3203 31.8526 B 425 LEU 20.1433 18.3272 1.8162 B 426 PRO 95.2197 47.9729 47.2468 B 427 ARG 75.8053 12.6035 63.2017 B 428 ALA 29.9192 13.4376 16.4816 B 429 LEU 0.6655 0.2491 0.4164 B 430 MET 94.7862 13.9214 80.8648 B 431 ARG 61.2436 10.0257 51.2179 B 432 SER 65.6617 25.5585 40.1032 B 433 THR 13.0233 5.6973 7.3260 B 434 THR 46.6839 7.5817 39.1022 B 435 LYS 48.5670 13.2907 35.2763 B 436 THR 47.1262 7.7492 39.3770 B 437 SER 93.7617 15.6507 78.1110 B 438 GLY 47.1648 47.1648 0.0000 B 439 PRO 92.2539 11.4315 80.8224 B 440 ARG 86.4119 32.6025 53.8094 B 441 ALA 41.0049 5.6703 35.3346 B 442 ALA 46.7251 10.6945 36.0306 B 443 PRO 4.7646 4.7646 0.0000 B 444 GLU 32.6629 0.1921 32.4708 B 445 VAL 1.9628 0.1088 1.8541 B 446 TYR 12.1809 1.1154 11.0655 B 447 ALA 19.0771 18.8089 0.2682 B 448 PHE 32.2261 5.3355 26.8906 B 449 ALA 26.3527 17.5706 8.7821 B 450 THR 8.1738 2.2896 5.8842 B 451 PRO 76.5842 4.9904 71.5938 B 452 GLU 93.8169 13.0331 80.7838 B 453 TRP 95.9141 1.6990 94.2151 B 454 PRO 125.8288 36.9609 88.8679 B 455 GLY 65.7610 65.7610 0.0000 B 456 SER 42.7528 8.4299 34.3229 B 457 ARG 182.0093 19.8205 162.1888 B 458 ASP 66.4899 1.5486 64.9413 B 459 LYS 148.5472 12.9959 135.5513 B 460 ARG 41.5604 3.1133 38.4471 B 461 THR 13.2538 1.6604 11.5934 B 462 LEU 6.3258 0.0649 6.2610 B 463 ALA 11.5779 0.4739 11.1040 B 464 CYS 1.0391 1.0391 0.0000 B 465 LEU 2.3588 0.0000 2.3588 B 466 ILE 0.3683 0.0000 0.3683 B 467 GLN 4.2086 0.0000 4.2086 B 468 ASN 35.9496 5.2065 30.7431 B 469 PHE 0.0000 0.0000 0.0000 B 470 MET 32.7360 0.0000 32.7360 B 471 PRO 9.7948 6.3053 3.4896 B 472 GLU 88.4549 3.7638 84.6910 B 473 ASP 47.2351 6.8458 40.3893 B 474 ILE 29.1817 24.1296 5.0520 B 475 SER 14.3571 4.1523 10.2049 B 476 VAL 20.6222 18.5324 2.0898 B 477 GLN 10.6533 0.0000 10.6533 B 478 TRP 1.8912 1.0361 0.8551 B 479 LEU 28.2585 0.9455 27.3131 B 480 HIS 9.7124 1.2163 8.4961 B 481 ASN 54.6134 14.8060 39.8074 B 482 GLU 172.9182 41.2890 131.6292 B 483 VAL 80.4369 2.9369 77.5000 B 484 GLN 86.7995 23.2392 63.5604 B 485 LEU 20.1440 8.7226 11.4214 B 486 PRO 79.3531 10.9230 68.4300 B 487 ASP 113.7037 8.5271 105.1766 B 488 ALA 105.1557 42.1652 62.9905 B 489 ARG 78.5174 20.7364 57.7810 B 490 HIS 27.7987 16.2252 11.5735 B 491 SER 30.5621 5.9459 24.6161 B 492 THR 40.2793 15.9582 24.3211 B 493 THR 12.2109 4.6417 7.5692 B 494 GLN 99.8352 2.7394 97.0958 B 495 PRO 38.5051 18.8569 19.6482 B 496 ARG 86.5718 5.6625 80.9093 B 497 LYS 159.5251 21.1005 138.4247 B 498 THR 19.4014 18.8518 0.5496 B 499 LYS 201.9754 42.6147 159.3607 B 500 GLY 44.4883 44.4883 0.0000 B 501 SER 85.5433 25.6861 59.8572 B 502 GLY 1.9867 1.9867 0.0000 B 503 PHE 31.1871 0.0000 31.1871 B 504 PHE 1.5596 0.0598 1.4998 B 505 VAL 0.9708 0.0000 0.9708 B 506 PHE 3.7613 0.1850 3.5763 B 507 SER 0.6262 0.0195 0.6068 B 508 ARG 9.5731 1.8218 7.7513 B 509 LEU 0.7046 0.0000 0.7046 B 510 GLU 62.9883 2.0494 60.9388 B 511 VAL 10.8762 6.5365 4.3397 B 512 THR 71.0071 0.0263 70.9809 B 513 ARG 104.2393 0.0000 104.2393 B 514 ALA 65.4206 13.1707 52.2499 B 515 GLU 35.3933 0.3618 35.0315 B 516 TRP 39.6550 3.3357 36.3193 B 517 GLU 115.3847 37.2436 78.1411 B 518 GLN 113.6505 33.6727 79.9778 B 519 LYS 84.0921 8.7130 75.3791 B 520 ASP 64.5129 2.3376 62.1754 B 521 GLU 87.5584 2.3918 85.1666 B 522 PHE 9.6600 0.0000 9.6600 B 523 ILE 30.2820 0.0000 30.2820 B 524 CYS 0.0000 0.0000 0.0000 B 525 ARG 37.1783 0.0000 37.1783 B 526 ALA 0.3818 0.3818 0.0000 B 527 VAL 0.0418 0.0000 0.0418 B 528 HIS 0.6191 0.1432 0.4759 B 529 GLU 49.1816 17.5861 31.5955 B 530 ALA 25.6926 20.8074 4.8853 B 531 ALA 7.1284 6.1152 1.0132 B 532 SER 92.9571 24.3505 68.6065 B 533 PRO 129.7170 30.9019 98.8150 B 534 SER 65.6135 12.1706 53.4428 B 535 GLN 60.5061 0.0227 60.4835 B 536 THR 22.1684 5.5560 16.6125 B 537 VAL 29.6659 6.3253 23.3407 B 538 GLN 69.4992 13.4096 56.0896 B 539 ARG 92.2922 3.4257 88.8665 B 540 ALA 62.4168 19.4066 43.0101 B 541 VAL 19.1443 12.3199 6.8244 B 542 SER 49.6556 19.3884 30.2672 B 543 VAL 20.6069 2.0847 18.5222 B 544 ASN 178.7782 70.1438 108.6343 B 694 NAG 107.4774 0.0000 107.4774 B 695 NAG 119.4719 0.0000 119.4719 B 696 MAN 45.7067 0.0000 45.7067 B 697 MAN 152.8463 0.0000 152.8463 B 698 MAN 222.3243 0.0000 222.3243 B 699 MAN 217.3122 0.0000 217.3122 D 329 CYS 102.3809 67.5332 34.8476 D 330 ASP 111.3542 32.4992 78.8550 D 331 SER 49.5069 8.1508 41.3561 D 332 ASN 19.9483 7.1538 12.7945 D 333 PRO 20.7718 9.3148 11.4570 D 334 ARG 103.0460 10.1992 92.8468 D 335 GLY 3.3799 3.3799 0.0000 D 336 VAL 12.9305 10.8477 2.0827 D 337 SER 17.9779 5.3981 12.5798 D 338 ALA 2.9541 2.7192 0.2349 D 339 TYR 68.8053 3.1433 65.6620 D 340 LEU 28.1176 26.0926 2.0250 D 341 SER 59.6285 9.0359 50.5926 D 342 ARG 87.3522 11.5821 75.7702 D 343 PRO 7.5238 7.5238 0.0000 D 344 SER 36.9529 6.5208 30.4322 D 345 PRO 11.5386 3.1229 8.4157 D 346 PHE 45.5005 0.0000 45.5005 D 347 ASP 47.0584 0.0024 47.0561 D 348 LEU 9.0480 0.3353 8.7126 D 349 PHE 22.9831 9.2421 13.7410 D 350 ILE 57.3966 13.5038 43.8927 D 351 ARG 140.1074 22.9695 117.1379 D 352 LYS 139.7937 14.7242 125.0695 D 353 SER 48.1517 7.3618 40.7899 D 354 PRO 3.2206 0.8205 2.4000 D 355 THR 54.2972 11.4293 42.8679 D 356 ILE 0.4144 0.4144 0.0000 D 357 THR 39.9578 1.7071 38.2507 D 358 CYS 0.3097 0.0000 0.3097 D 359 LEU 18.5271 0.0018 18.5253 D 360 VAL 1.3679 0.0000 1.3679 D 361 VAL 0.3469 0.0000 0.3469 D 362 ASP 12.4469 6.3831 6.0638 D 363 LEU 4.9868 1.6440 3.3428 D 364 ALA 19.9780 5.4292 14.5488 D 365 PRO 65.0465 6.1738 58.8727 D 366 SER 32.8048 26.7953 6.0096 D 367 LYS 136.0098 36.9049 99.1049 D 368 GLY 26.7169 26.7169 0.0000 D 369 THR 93.8010 14.7194 79.0816 D 370 VAL 15.1817 1.2150 13.9667 D 371 ASN 71.4877 1.7213 69.7664 D 372 LEU 27.5581 21.2832 6.2749 D 373 THR 64.9412 3.5271 61.4141 D 374 TRP 21.6411 12.7579 8.8832 D 375 SER 45.5983 4.0264 41.5719 D 376 ARG 46.1407 18.3951 27.7456 D 377 ALA 73.2052 42.7392 30.4661 D 378 SER 60.9391 42.2524 18.6867 D 379 GLY 62.4810 62.4810 0.0000 D 380 LYS 114.3210 4.9018 109.4192 D 381 PRO 118.6128 19.3560 99.2568 D 382 VAL 56.2105 27.7078 28.5027 D 383 ASN 89.7140 9.4333 80.2807 D 384 HIS 175.3907 15.2111 160.1796 D 385 SER 60.1172 34.0544 26.0628 D 386 THR 63.3471 6.6705 56.6765 D 387 ARG 100.5610 32.1288 68.4323 D 388 LYS 117.6302 8.3122 109.3179 D 389 GLU 93.9137 30.6429 63.2707 D 390 GLU 96.2332 5.9265 90.3067 D 391 LYS 170.3439 24.4483 145.8956 D 392 GLN 31.5360 6.5112 25.0248 D 393 ARG 229.7092 34.9960 194.7132 D 394 ASN 71.2822 36.9290 34.3532 D 395 GLY 54.2216 54.2216 0.0000 D 396 THR 14.4859 6.7168 7.7691 D 397 LEU 31.2188 0.0000 31.2188 D 398 THR 0.9937 0.0352 0.9584 D 399 VAL 1.8265 0.0023 1.8242 D 400 THR 28.8418 0.0000 28.8418 D 401 SER 1.8342 0.0000 1.8342 D 402 THR 38.4300 1.3612 37.0688 D 403 LEU 1.3700 0.0000 1.3700 D 404 PRO 56.4630 5.0109 51.4521 D 405 VAL 10.3785 9.6144 0.7642 D 406 GLY 19.9415 19.9415 0.0000 D 407 THR 17.7730 0.0342 17.7388 D 408 ARG 149.6237 4.1119 145.5118 D 409 ASP 52.0866 6.4418 45.6449 D 410 TRP 13.1899 0.0000 13.1899 D 411 ILE 63.5723 7.3792 56.1932 D 412 GLU 148.7782 36.0783 112.6999 D 413 GLY 38.9396 38.9396 0.0000 D 414 GLU 20.8518 6.7344 14.1173 D 415 THR 39.3540 0.6913 38.6627 D 416 TYR 5.8935 0.0014 5.8921 D 417 GLN 62.2903 0.0009 62.2895 D 418 CYS 0.4753 0.3779 0.0974 D 419 ARG 106.4535 0.4475 106.0060 D 420 VAL 2.7864 0.0595 2.7269 D 421 THR 47.3939 3.4111 43.9828 D 422 HIS 13.1471 8.0455 5.1016 D 423 PRO 73.2651 38.6918 34.5733 D 424 HIS 5.0313 3.9403 1.0910 D 425 LEU 26.2169 16.8989 9.3180 D 426 PRO 16.7230 16.7230 0.0000 D 427 ARG 90.3191 7.4734 82.8457 D 428 ALA 36.2453 22.9999 13.2454 D 429 LEU 33.6211 0.8879 32.7333 D 430 MET 81.2915 16.0381 65.2534 D 431 ARG 95.2832 10.2332 85.0500 D 432 SER 62.4521 22.5286 39.9235 D 433 THR 16.4152 7.6464 8.7688 D 434 THR 43.2290 5.7565 37.4725 D 435 LYS 48.4737 13.5566 34.9171 D 436 THR 40.0113 7.5864 32.4249 D 437 SER 92.1976 14.6061 77.5915 D 438 GLY 47.1703 47.1703 0.0000 D 439 PRO 87.5094 11.3492 76.1603 D 440 ARG 91.1554 32.4332 58.7222 D 441 ALA 37.6064 5.6168 31.9896 D 442 ALA 47.7716 10.8839 36.8877 D 443 PRO 4.7444 4.7444 0.0000 D 444 GLU 31.7469 0.2472 31.4997 D 445 VAL 2.2316 0.4056 1.8260 D 446 TYR 13.0081 1.2161 11.7920 D 447 ALA 19.3686 19.1556 0.2130 D 448 PHE 32.4618 5.0174 27.4445 D 449 ALA 26.4564 17.8510 8.6054 D 450 THR 6.7460 1.4957 5.2504 D 451 PRO 78.1205 5.0753 73.0452 D 452 GLU 98.7545 13.9213 84.8332 D 453 TRP 95.8047 1.7250 94.0797 D 454 PRO 125.4561 37.0254 88.4307 D 455 GLY 65.7398 65.7398 0.0000 D 456 SER 42.2645 8.7091 33.5554 D 457 ARG 185.3827 19.6535 165.7292 D 458 ASP 64.7836 1.4527 63.3309 D 459 LYS 150.1746 13.4092 136.7655 D 460 ARG 41.0497 3.6090 37.4407 D 461 THR 12.7243 1.3702 11.3540 D 462 LEU 5.8977 0.0000 5.8977 D 463 ALA 9.3450 0.3148 9.0302 D 464 CYS 0.6992 0.6992 0.0000 D 465 LEU 2.3713 0.0565 2.3149 D 466 ILE 0.3495 0.0005 0.3490 D 467 GLN 5.5766 0.0000 5.5766 D 468 ASN 37.3320 5.0478 32.2843 D 469 PHE 0.0020 0.0020 0.0000 D 470 MET 31.1122 0.0000 31.1122 D 471 PRO 7.4404 4.3666 3.0739 D 472 GLU 83.9660 3.9591 80.0069 D 473 ASP 40.3144 6.4854 33.8290 D 474 ILE 29.6267 24.7486 4.8781 D 475 SER 15.2528 4.1160 11.1368 D 476 VAL 20.2396 18.2215 2.0182 D 477 GLN 12.4429 0.0027 12.4403 D 478 TRP 1.7703 0.9849 0.7854 D 479 LEU 28.1196 1.0451 27.0745 D 480 HIS 9.4122 1.1137 8.2985 D 481 ASN 56.0442 16.0061 40.0381 D 482 GLU 170.6455 41.2302 129.4154 D 483 VAL 80.9853 2.7860 78.1993 D 484 GLN 88.3797 22.1725 66.2072 D 485 LEU 20.3000 9.0697 11.2303 D 486 PRO 79.3386 10.6028 68.7358 D 487 ASP 114.5014 8.7729 105.7285 D 488 ALA 104.3458 41.8161 62.5297 D 489 ARG 79.9265 20.4064 59.5200 D 490 HIS 27.6480 16.2092 11.4388 D 491 SER 29.4802 5.4279 24.0523 D 492 THR 40.7927 16.2337 24.5591 D 493 THR 11.8506 4.3668 7.4838 D 494 GLN 119.5958 2.8589 116.7369 D 495 PRO 39.1911 18.6929 20.4981 D 496 ARG 86.9475 5.7213 81.2261 D 497 LYS 160.3208 19.6386 140.6822 D 498 THR 18.7636 18.4350 0.3286 D 499 LYS 200.0818 42.2517 157.8301 D 500 GLY 44.5668 44.5668 0.0000 D 501 SER 86.6338 25.9131 60.7207 D 502 GLY 1.8767 1.8767 0.0000 D 503 PHE 31.3369 0.0034 31.3334 D 504 PHE 1.4032 0.0633 1.3399 D 505 VAL 0.8780 0.0000 0.8780 D 506 PHE 4.3508 0.1793 4.1714 D 507 SER 0.5298 0.0000 0.5298 D 508 ARG 8.9714 1.8540 7.1174 D 509 LEU 0.7079 0.0000 0.7079 D 510 GLU 61.8196 1.9056 59.9140 D 511 VAL 10.8929 6.6139 4.2790 D 512 THR 71.8291 0.0838 71.7453 D 513 ARG 105.1744 0.0000 105.1744 D 514 ALA 65.9787 13.5900 52.3887 D 515 GLU 36.2623 0.0481 36.2142 D 516 TRP 40.1069 3.3758 36.7311 D 517 GLU 115.7130 37.9922 77.7208 D 518 GLN 110.4985 32.2394 78.2591 D 519 LYS 84.2805 8.6356 75.6448 D 520 ASP 65.1989 2.2319 62.9670 D 521 GLU 87.5054 1.9237 85.5818 D 522 PHE 9.4572 0.0000 9.4572 D 523 ILE 31.1442 0.0000 31.1442 D 524 CYS 0.0003 0.0003 0.0000 D 525 ARG 39.5175 0.0000 39.5175 D 526 ALA 0.4314 0.4314 0.0000 D 527 VAL 0.1473 0.0000 0.1473 D 528 HIS 0.6558 0.1273 0.5285 D 529 GLU 49.3913 17.1907 32.2006 D 530 ALA 25.8310 20.8648 4.9662 D 531 ALA 6.3430 5.3376 1.0054 D 532 SER 90.9851 24.3589 66.6262 D 533 PRO 129.9180 31.2948 98.6232 D 534 SER 63.8534 10.9652 52.8881 D 535 GLN 62.1692 0.1376 62.0316 D 536 THR 20.7628 5.8645 14.8983 D 537 VAL 29.9134 6.1442 23.7692 D 538 GLN 73.2944 13.0975 60.1969 D 539 ARG 94.0071 3.3512 90.6559 D 540 ALA 62.7499 19.2166 43.5333 D 541 VAL 20.0580 13.1091 6.9490 D 542 SER 52.5909 21.4389 31.1520 D 543 VAL 20.1018 2.8350 17.2667 D 544 ASN 177.6491 71.3693 106.2798 D 694 NAG 136.0235 0.0000 136.0235 D 695 NAG 128.7899 0.0000 128.7899 D 696 MAN 176.7398 0.0000 176.7398 E 101 CPS 163.2849 0.0000 163.2849 E 102 CHA 333.1883 0.0000 333.1883 E 103 CPS 83.0589 0.0000 83.0589 E 104 CPS 313.3217 0.0000 313.3217 E 105 CPS 246.4972 0.0000 246.4972

[0040] Residues that are solvent accessible are important as they represent amino acids that are on the external surface of the proteins in the complex and, as such, may be involved in binding of a FcR to an antibody and as such be useful in designing proteins with an enhanced binding activity or in identifying compounds that inhibit such binding. In addition, solvent accessible residues can represent targets for modification to produce a FcR or antibody with improved function. Such analysis also identifies residues in the interior, or core, of the proteins in the complex. Such residues can also be targeted to produce proteins with improved functions, such as enhanced stability.

[0041] A model of the present invention also provides additional information that is not available from other sources. For example, a model can identify the crystal contacts between crystals and predict the location of the IgE binding domain, including those amino acids that actually form contacts with a Fc domain of an IgE antibody, such as those in the binding face of the FcεRIα protein. A model can also identify the amino acids in the interface between domain 1 and domain 2 (i.e., the D1D2 interface), as well as those in the cleft formed between the two domains of the FcεRIα protein. Particularly important regions of the complex indicated by the model represented in Table 1 include, but are not limited to, FcεRIα:Fc-Cε3/Cε4 interaction site 1, FcεRIα:Fc-Cε3/Cε4 interaction site 2, the hinge between domain Cε3 and domain Cε4 of the Fc-Cε3/Cε4 region, and a FcERIa:Fc-Cε3/Cε4 region that interacts with 3-[3-(cholamidopropyl) dimethylammonio]-1-propane-sulfonate (CHAPS). Interaction sites 1 and 2 are the sites at which amino acids from FcεRIα and Fc-Cε3/Cε4 interact with each other. These sites are described in more detail in the Examples and represent sites to target for drug design and mutein production.

[0042] One embodiment of the present invention is a model that represents a complex that includes a protein that binds to a Fc domain of an IgE antibody with an affinity that is at least equivalent to the affinity of the extracellular domain of human FcεRIα for any one of the following IgE antibodies: a human IgE antibody, a canine IgE antibody, a feline IgE antibody, an equine IgE antibody, a rat IgE antibody, and a murine IgE antibody. Such a model can represent an extracellular domain of a human FcεRIα protein, a canine FcεRIα protein, a feline FcεRIα protein, an equine FcεRIα protein, a murine FcεRIα protein, and a rat FcεRIα protein. Such a model can also represent a protein with altered substrate specificity, preferably designed based on a model of the present invention. WO 98/23964, ibid., reports the ability of an isolated human FcαRIα protein to bind to canine, feline and equine IgE antibodies. Models of the present invention can be used to design a FcR with increased affinity for an antibody of a species other than self, such as, but not limited to, a human FcεRIα with increased affinity for a canine, feline or equine IgE antibody.

[0043] A model of the present invention can also represent a complex that includes a Fc domain of an antibody that binds to a FcεRIα protein with an affinity that is at least equivalent to the affinity of a human IgE antibody Fc-Cε3/Cε4 region for the extracellular domain of any of the following FcεRIα proteins: a human FcεRIα protein, a canine FcεRIα protein, a feline FcεRIα protein, an equine FcαRIα protein, a murine FcεRIα protein and a rat FcεRIα protein. Such a model can represent a FceRI-binding domain of a human, canine, feline, equine, murine or rat Fe region. Such a model can also represent a Fe region with altered substrate specificity, preferably designed based on a model of the present invention.

[0044] The present invention includes a model that represents a complex between a FcR and a Fe domain that binds to an antibody or receptor of its respective class (i.e., IgE, IgG, IgM, IgA or IgD antibody class or corresponding Fe receptor). Also included is a model that represents a complex between a FcR and antibody designed to bind to an antibody or receptor, respectively, of a class other than the class to which the protein naturally binds. Such a model of the present invention can be produced, for example, by incorporating all or any part of the amino acid sequence of the other FcR or antibody into a 3-D model substantially representing the coordinates in Table 1. Such an embodiment includes any model that specifically incorporates any Ig domains that are placed in an orientation (packing interfaces and bend angles) that is based on the structure of the FcεRI or a model that is based on the 1:1 stoichiometry predicted by the coordinates in Table 1. A preferred model of the present invention represents a complex including a FcR that binds to an IgE antibody or to an IgG antibody. In one embodiment, a model of the present invention is a 3-D model of a complex between an extracellular antibody binding domain of a FcR other than human FcεRIα, such as of a FcR that binds to an IgG antibody and an antibody. Such proteins and models thereof can be designed by homology modeling by, for example, altering the substrate specificity of a FcεRIα protein such that the altered protein binds an IgG antibody.

[0045] A preferred modified model of the present invention is a model that has a 3-D structure comprising atomic coordinates that have a root mean square deviation of protein backbone atoms of less than 10 angstrom when superimposed, using backbone atoms, on the 3-D model substantially represented by the atomic coordinates specified in Table 1. Preferably such a model has a 3-D structure comprising atomic coordinates that have a root mean square deviation of protein backbone atoms of less than 8 angstroms, preferably less than 7 angstroms, preferably less than 6 angstroms, preferably less than 5 angstroms, preferably less than 4 angstroms, preferably less than 3 angstroms, preferably less than 2 angstroms, and preferably less than 1 angstroms, when superimposed, using backbon3 atoms, on the 3-D model substantially represented by the atomic coordinates specified in Table 1. In this embodiment, such a model represents a FcR binding to an antibody. The backbone atoms are those atoms that form the backbone, or 3-D folding pattern, of the model. As such, backbone atoms are the base residues of amino acids, i.e., nitrogen, carbon, the alpha carbon and oxygen. Also preferred is a model modification that includes (a) a FcR protein having an amino acid sequence that shares at least about 30%, preferably at least about 40%, more preferably at least about 45%, more preferably at least about 50%, more preferably at least about 60% and even more preferably at least about 80% amino acid sequence homology, with a human FcεRIα protein, as determined using the program ALIGN with default parameters, optimal global alignment of two sequences with no short-cuts and (b) a Fc region having an amino acid sequence that shares at least about 30%, preferably at least about 40%, more preferably at least about 45%, more preferably at least about 50%, more preferably at least about 60% and even more preferably at least about 80% amino acid sequence homology, with a Fc-Cε3/Cε4 region of a human IgE antibody, as determined using the program ALIGN with default parameters, optimal global alignment of two sequences with no short-cuts. It is to be noted that, using the same program and parameters, the extracellular domain of a human FcεRIα protein (i.e., soluble human FcεRIα protein) shares about 48% identity with feline and rat soluble FcεRIα proteins, about 49% with a murine soluble FcεRIα protein, about 50% identity with a canine soluble FcεRIα protein, and about 60% identity with an equine soluble FcεRIα protein. A preferred model of the present invention represents an IgE binding domain, i.e., a region that binds to an IgE antibody, complexed to a FcεRIα-binding domain, i.e., a region that binds to a FcεRIα protein.

[0046] One embodiment of the present invention is a 3-D model of a complex between a human FcεRIα protein and a human Fc-Cε3/Cε4 region produced by a method that includes the steps of: (a) crystallizing a complex between an extracellular domain of a human FcεRIα protein, such as, but not limited to a protein having amino acid sequence SEQ ID NO:2 or SEQ ID NO:4 and a human Fc-Cε3/Cε4 region, such as, but not limited to a protein having amino acid sequence SEQ ID NO:6; (b) collecting X-ray diffraction data from the crystallized complex; and (c) determining the model from the X-ray diffraction data, preferably in combination with an amino acid sequence of the proteins in the complex. A complex for crystal formation can be produced using a variety of techniques well known to those skilled in the art. As disclosed herein, human FcεRIα proteins and human Fc-Cε3/Cε4 region sto be crystallized are preferably produced in recombinant insect cells transformed with a gene encoding the respective proteins, such as a baculovirus genetically engineered to produce the respective protein. The purity of the FcεRIα protein or Fc-Cε3/Cε4 region must be sufficient to permit the production of crystals that can be analyzed by X-ray crystallography to a resolution that permits determination of a 3-D model of the protein. Preferably the resolution is at least about 4.5 angstroms (i.e., 4.4 angstroms or better), more preferably at least about 4 angstroms, more preferably at least about 3.5 angstroms, more preferably at least about 3.25 angstroms, more preferably at least about 3 angstroms, more preferably at least about 2.5 angstroms, more preferably at least about 2 angstroms and even more preferably at least about 1.5 angstroms. Methods to obtain such purity levels are well known to those skilled in the art.

[0047] As disclosed herein, a preferred method to crystallize a complex between a FcεRIα protein and a Fc-Cε3/Cε4 region is by vapor distillation. Particularly preferred methods are disclosed in the Examples. It should be appreciated that the present invention also includes other methods known to those skilled in the art by which such a complex can be crystallized.

[0048] 3-D models of some proteins have been determined; see, for example, Blundell et al., Protein Crystallography, Academic Press, London, 1976. However, as discussed herein, elucidation of the crystal structure of a complex between the extracellular domain of the human FcεRIα and a Fc-Cε3/Cε4 region of a human IgE was difficult. In one embodiment, crystal structure determination includes obtaining high-resolution data using synchrotron radiation. Such data can be collected, for example, at the Stanford Synchrotron Source Laboratory, Palo Alto, Calif., or the Advanced Photon Source at Argonne National Laboratories, Argonne, Ill. Additional locations to collect such data include, but are not limited to, Brookhaven, N.Y., and Japan. In one embodiment, diffraction data from native and heavy-atom treated crystals provide an initial image of the protein structure which is refined into an electron density map. Details regarding data collection and interpretation are provided in the Examples section.

[0049] One embodiment of the present invention is a method to produce a 3-D model of a FcεRIα protein that includes positioning amino acid representations (i.e., representing amino acids) of the protein at substantially the coordinates listed in Table 1. That is, knowledge of the coordinates of the complex permits one skilled in the art to produce a model of the complex using those coordinates. Such a model, or any model which is essentially represented by a simple coordinate transformation of the coordinates specified in Table 1, can be represented in a variety of methods as heretofore disclosed and is included in the present invention.

[0050] In another embodiment, a model of the present invention can be refined to obtain an improved model, which is an example of a model modification, also referred to as a modified model. Refining methods can include, but are not limited to, further data collection and analysis; data collection from frozen crystals; introduction of solvent molecules to the structure; clarification of secondary structure; and analyses of crystallized complexes between a FcR and an antibody or inhibitory compound or of crystallized FcRs or antibodies alone. An additional model refinement method includes analyzing a 3-D model to predict amino acid residues that if replaced are likely to yield proteins with at least one improved function, effecting at least one such replacement, determining whether the activity of the modified protein agrees with the prediction, and refining the model as necessary. Methods to determine whether the modification agrees with prediction include producing the modified protein and performing assays with that modified protein to determine if the protein does indeed exhibit the improved function(s), such as desired activity, stability and solubility properties. Assays to measure such functions are well known in the art; examples of several such assays are disclosed herein.

[0051] Another embodiment of the present invention is a modified 3-D model that represents a complex between a FcR other than a human FcεRIα protein represented by the 3-D model the coordinates of which are listed in Table 1 and an antibody other than human IgE as represented by the coordinates in Table 1. Preferably the amino acid sequence of the protein(s) to be modeled is known. In such a case, the modified model can be produced using the technique of homology modeling, preferably by incorporating (e.g., grafting, overlaying or replacing) all or any portion of the amino acid sequence of the other FcR or antibody into the 3-D model representing the coordinates of Table 1 to produce the modified model. General techniques for homology modeling, also referred to as molecular replacement, have been disclosed in, for example, Greer, 1990, Proteins: Structure, Function, and Genetics 7, 317-334; Havel et al., 1991, J. Mol. Biol. 217, 1-7; Schiffer et al., 1990, Proteins: Structure, Function, and Genetics 8, 30-43; and Lattman, 1985, Methods Enzymol 115, 55-77. However, such technology has not been applied to complexes between FcRs and antibodies since, until the present invention, no 3-D model of any FcR:antibody complex was available. Thus, the present invention now allows the solving of the structures of a number of other natural and mutated forms of FcRs, antibodies or complexes thereof.

[0052] In one embodiment, a model of a FcR:Fc complex, such as, but not limited to a FcεRIα:Fc-Cε3/Cε4 complex, is produced by extracting the 3-D coordinates from a published figure or building a 3-D model with atoms from other domains wherein the domain 1 and 2 of the FcR and FcR-binding domains of the antibody are oriented as predicted for a complex between the human FcεRIα₁₋₁₇₆ protein and human Fc-Cε3/Cε4₂₂₂ protein. For example, a model of the present invention can be produced by orienting two known Ig domains into a bent confirmation similar to that of the two domains of the human FcεRIα protein. Such a model is referred to as a model in which domain 1 and domain 2 are oriented in a manner as specified by the structural coordinates listed in Table 1. This model can then be used in further molecular replacement methods. Such methods can include the steps of (a) orienting the model by three rotations; and (b) translating the model in one to three directions to produce additional model modifications.

[0053] Suitable FcRs or antibodies for which a 3-D model can be determined using homology modeling include any mammalian FcR or antibody, such as a protein that binds to IgE, IgG, IgM, IgA or IgD antibodies or an antibody that binds to the corresponding FcR. Preferred is a FcR protein that binds to an IgE antibody or an IgG antibody. Preferred FcRs that bind to IgE include human, canine, feline, equine, murine and rat FcεRIα proteins. Preferred antibodies that bind to FcRs include human, canine, feline, equine, murine and rat antibodies. The present invention also includes the use of other Ig domains to produce models of the present invention.

[0054] One embodiment of the present invention is a 3-D model of a FcR:antibody complex in which one or both proteins have an improved function compared to an unmodified protein as well as a method to produce such a modified model. Such an improved function includes, but is not limited to, enhanced activity, enhanced stability and enhanced solubility. Such a modified model can be produced by replacing at least one amino acid based on information derived from analyzing the 3-D model representing the coordinates in Table 1, such that the replacement leads to a protein with an improved function. As used herein, a replacement refers to an (i.e., one or more) amino acid substitution, insertion, deletion, inversion and/or derivatization (e.g., acetylation, glycosylation, phosphorylation, PEG modification, biotinylation, and covalent attachment of other ligands or other compounds to the protein. In one embodiment, synthetic chemical methods are used to produce either a fragment or the entire protein to, for example, introduce non-natural amino acids or other chemical compounds into the structure of a FcR or antibody. For example, based on a structure of the present invention, one can design synthetic peptides or larger proteins that could be linked to produce an intact protein with IgE or FcR binding activity, the structure allowing one to design the start and stop points for these peptides, e.g., at surface accessible loops. In accordance with the present invention, an amino acid that is substituted or inserted can be a natural amino acid or an unnatural amino acid, including a derivitized amino acid. Methods to identify regions in the protein that, if changed, yield a protein with an improved function are disclosed below.

[0055] The present invention includes use of a 3-D model of the present invention to identify a compound that inhibits binding between a FcR and an antibody. The advantages of using a 3-D model to identify inhibitory compounds are multi-fold in that the model depicts the site at which a Fc region of an antibody binds to its FcR, i.e., the antibody-binding domain, also referred to as the antibody binding site, and the FcR-binding domain, also referred to as the FcR binding site. The antibody binding site and the FcR binding site together form an FcR:antibody interaction site. As such, a large number of potential inhibitory compounds can be initially analyzed without having to perform in vitro or in vivo laboratory studies. As used herein, methods to identify inhibitory compounds include, but are not limited to, designing inhibitory compounds based on the 3-D model of a FcR, probing such a 3-D model with compounds that are potential inhibitors in order to identify those compounds that are actually inhibitory of the binding of an antibody to its FcR, screening a compound data base using such a 3-D model to identify compounds that inhibit such binding, and combinations thereof. Methods to use 3-D models to design, probe for, or screen for suitable inhibitory compounds are known to those skilled in the art. In particular, there are a number of computer programs that enable such methods. See, for example, PCT Publication No. WO 95/35367, by Wilson et al., published Dec. 28, 1995, which is incorporated by reference herein in its entirety.

[0056] An inhibitory compound can be any natural or synthetic compound that inhibits the binding of an antibody to a FcR. Examples include, but are not limited to, inorganic compounds, oligonucleotides, proteins, peptides, antibodies, antibody fragments, mimetics of peptides or antibodies (such as, mimetics of antibody or receptor binding sites), and other organic compounds. Compounds can inhibit binding in either a competitive or non-competitive manner and can either interact at the binding site or allosterically. An inhibitory compound should be capable of physically and structurally associating with a FcR and/or an antibody such that the compound can inhibit binding between the two entitites. As such, an inhibitory compound is preferably small and is of a structure that effectively prevents or disrupts binding. Inhibitory compounds can be identified in one or multiple steps. For example, a compound initially identified that inhibits binding between an antibody and FcR to some extent can be used as a lead to design, probe or screen for a compound with improved characteristics, such as greater efficacy, safety, solubility, etc. A preferred inhibitory compound is a compound that is efficacious when administered to an animal in an amount that results in a serum concentration of from about 1 nanomolar (nM) to 100 micromolar (mM), with a concentration of from about 10 nM to 10 mM being more preferred.

[0057] One embodiment of the present invention is a method to identify a compound that inhibits the binding between an IgE antibody and a FcεRIα protein. Such a method includes the step of using a 3-D model substantially representing the atomic coordinates specified in Table 1 to identify such a compound. Included in the present invention are inhibitory compounds that interact directly with the IgE binding domain or the receptor binding domain of the IgE antibody as well as compounds that interact indirectly with an FcεRIα protein, such as compounds that interact with the IgE binding domain, the FcεRIα binding domain, FcεRIα:Fc-Cε3/Cε4 interaction site 1, FcεRIα:Fc-Cε3/Cε4 interaction site 2, the hinge between domain Cε3 and domain Cε4 of the Fc-Cε3/Cε4 region, or a FcεRIα:Fc-Cε3/Cε4 region that interacts with CHAPS. In a preferred embodiment, an inhibitory compound interacts with at least one of the following regions of a model representing a FcεRIα:Fc-Cε3/Cε4 complex: a C strand of domain 2 of FcεRIα, a C′E loop of domain 2 of FcεRIα, a tryptophan-containing hydrophobic ridgeof FcεRIα, a linker between domain 1 and domain 2 of FcεRIα, a BC loop of domain 2 of FcεRIα, a FG loop of domain 2 of FcεRIα, a Cε2/Cε3 linker region of Fc-Cε3/Cε4, a BC loop of Fc-Cε3/Cε4, a DE loop of Fc-Cε3/Cε4, and a FG loop of Fc-Cε3/Cε4. Inhibitory compounds of the present invention preferably interact with at least one of the following amino acids: (a) a residue having a position in SEQ ID NO:2 selected from the group consisting of position 85, 86, 87, 110, 113, 117, 119, 126, 129, 130, 131, 132, 156, 157, and 158; (b) a residue having a position in SEQ ID NO:6 selected from the group consisting of position 4, 7, 8, 9, 10, 11, 37, 38, 39, 68, 69, 70, 99, 100, 101 and 102; and (c) a surface residue within about 10 angstroms of any of the residues listed in (a) or (b). Particularly preferred amino acids with which to interact are: (a) a residue within the FcεRIα pocket for the proline at position 101 of SEQ ID NO:6, such residues including, but not limited to positions 85, 86, 87 and 110 of SEQ ID NO:2; (b) a residue within the IgE pocket for the tyrosine at position 131 of SEQ ID NO:2, such residues including, but not limited to, positions 9, 11, 37, 39, and 99 of SEQ ID NO:6; and (c) a surface residue within about 10 angstroms of any of said residues of (a) or (b). It is to be noted that the ability to identify such key regions and residues is only possible in view of a model of the present invention. These regions and residues are a refinement of those identified using a FcεRIα model as described in 09/434,193, ibid. or WO 00/26246, ibid. In one embodiment, an inhibitory compound of the present invention is a peptide corresponding to at least a portion of any of the identified regions or a derivative thereof, such as a peptide mimetic or other compound that mimics that peptide.

[0058] One embodiment of a method to identify a compound that inhibits the binding between an IgE antibody and a FcεRIα protein includes the steps of: (a) generating a model substantially representing the atomic coordinates listed in Table 1 or of the binding domains thereof, on a computer screen; (b) generating the spacial structure of a compound to be tested; and (c) testing to determine if the compound interacts with said IgE binding domain or FcR binding domain, wherein such an interaction indicates that the compound is capable of inhibiting the binding of an IgE antibody to a FcεRIα protein. In a preferred embodiment, step (a) includes the step of identifying one or more amino acid(s) in the IgE binding domain of FcR binding domain of the model that interact directly with the corresponding domain. Preferably a compound to be tested will interact directly with one or more of those amino acid(s). Preferred amino acids with which an inhibitory compound should interact are disclosed herein.

[0059] The present invention also includes inhibitory compounds isolated in accordance with the methods disclosed herein. Methods to produce such compounds in quantities sufficient for use, for example, as protective agents (e.g., preventatives or therapeutics) are known to those skilled in the art. It should also be appreciated that it is within the scope of the present invention to expand the use of models of the present invention to produce models of any suitable FcRs (i.e., model modifications) and to identify compounds that inhibit the binding of antibodies to such FcRs.

[0060] A preferred inhibitory compound of the present invention, or lead that can be used to produce a more efficacious inhibitory compound, is a saturated tetracyclic hydrocarbon perhydrocyclopentanophenanthrene or a derivative thereof. Such a compound can include a structure having the following formula:

[0061] It is to be understood that such a compound can have any number of “R” groups, even though they are not indicated in the formula. Examples of saturated tetracyclic hydrocarbon perhydrocyclopentanophenanthrenes include, but are not limited to, isoprenoids, terpenes, bile acids, detergents (such as CHAPS and CHAPSO) cholestanes, cholic acids, cholesterols, androgens, estrogens, and other steroids. A preferred inhibitory compound, or compound to use as a lead to design a more efficacious compound is 3-[3-(cholamidopropyl) dimethylammonio]-1-propane-sulfonate (CHAPS) or a compound having a similar ring structure. The interaction of CHAPS with amino acids in the FcεRIα protein and Fc-C3/C4 region is described in further detail in the Examples.

[0062] The present invention also includes use of a 3-D model of the present invention to rationally design and construct modified forms of FcRs or antibodies that have one or more improved functions, such as, but not limited to, increased activity, increased stability and increased solubility compared to an unmodified FcR or antibody. Muteins of the present invention include full-length proteins as well as fragments (i.e., truncated versions) of such proteins.

[0063] One embodiment of the present invention is a FcR that comprises a mutein that binds to a Fc domain of an antibody. Such a mutein has an improved function compared to a protein comprising SEQ ID NO:2. Examples of such an improved function include, but are not limited to, increased stability, increased affinity for an Fc domain of an antibody, altered substrate specificity, and increased solubility. Such a mutein can be produced by a method that includes the steps of: (a) analyzing a 3-D model substantially representing the atomic coordinates specified in Table 1 to identify at least one amino acid of the protein represented by the model which if replaced by a specified amino acid would effect the improved function of the protein; and (b) replacing the identified amino acid(s) to produce a mutein having the improved function. Knowledge of the coordinates allows one to target specific residues, e.g. in the hydrophobic core or on the surface, to generate an accessible set of variants that can then be selected for a particular property, e.g. high stability, high affinity, altered substrate specificity, or other desirable properties (i.e., improved functions). Without the coordinates, one would have to analyze an extraordinarily large number of variants, e.g., on the order of ˜10¹¹ possibilities. The structure, in contrast, allows one to pick the most relevant residues for selecting a desired property by, for example, phage display or other methods. In a preferred embodiment, replacement of one or more amino acids does not substantially disrupt the 3-D structure of the protein; i.e., the modified protein, or mutein, is still capable of binding to the Fc domain of an antibody. A preferred mutein is a FcR that binds to a Fe domain of an IgE antibody, although the invention also covers muteins binding to other classes of antibodies.

[0064] In one embodiment, a mutein of the present invention has increased stability compared to its unmodified counterpart. As used herein, increased stability refers to the ability of a mutein to be more resistant, for example, to higher or lower temperature, to more acidic or basic pH, to higher or lower salt concentrations, to oxidation and/or reduction, to deamidation, to other forms of chemical degradation and to proteolytic degradation compared to unmodified FcR. Increased stability can also refer to the ability of a mutein of the present invention to be stable for a longer period of time either during storage (i.e., to have a longer shelf life) or during use (i.e., to have a longer half-life under reaction conditions) than does an unmodified protein. Muteins of the present invention can also exhibit a decreased entropy of unfolding, thereby stabilizing the proteins. Increased stability can be measured using a variety of methods known to those skilled in the art; examples include, but are not limited to, determination of melting temperature, thermal denaturation, pressure denaturation, enthalpy of unfolding, free energy of the protein, or stability in the presence of a chaotropic agents such as urea, guanidinium chloride, guanidinium thiocyanate, etc. A preferred mutein of the present invention has a melting temperature substantially higher than that of an unmodified FcR. Preferably the melting temperature of a mutein is at least about 1° C. higher, and more preferably at least about 10° C. higher than the melting temperature of the corresponding unmodified protein. Also preferred is a mutein having binding activity over a pH range that is at least about 1 pH unit higher and/or lower than the active pH range of the corresponding unmodified protein.

[0065] Another embodiment of the present invention is a mutein that exhibits increased affinity for a Fc domain of an antibody compared to its unmodified counterpart. As used herein, a mutein having increased affinity is a FcR that exhibits a higher affinity constant (K_(A)) or lower dissociation constant (K_(D)) than its unmodified counterpart. Such a higher affinity constant can be achieved by increasing the association rate (k_(a)) between the mutein and the Fc domain and/or decreasing the dissociation rate (k_(d)) between the mutein and the Fc domain. A preferred mutein of the present invention has a K_(A) for a Fc domain of at least about 3×10⁹ liters/mole (M⁻¹), which is equivalent to a K_(D) of less than or equal to about 3.3×10⁻¹⁰ moles/liter (M). More preferred is a mutein having a K_(A) for a Fc domain of at least about 2×10¹⁰ M⁻¹, and even more preferably of at least about 1×10¹¹ M⁻¹. Also preferred is a mutein having a k_(a) for a Fc domain of at least about 1×10⁵ liters/mole-second as well as a mutein having a k_(d) for a Fc domain of less than or equal to 3×10⁻⁵/second. More preferred is a mutein having a k_(a) for a Fc domain of at least about 3×10⁵ liters/mole-second, and even more preferably of 1×10⁶ liters/mole-second. Also preferred are muteins having a k_(d) for a Fc domain of less than or equal to 1×10⁻⁵/second or even more preferably less than or equal to 3×10⁻⁴/second. A preferred Fc domain is that of an IgE antibody. Methods to measure such binding constants is well known to those skilled in the art; see, for example, Cook et al., 1997, ibid., which reports the following values for the binding of human FcεRIα protein to human IgE: k_(a1) of 3.5 (±0.9)×10 ⁵ M⁻¹s⁻¹; k_(a2) of 8.6 (±3.5)×10⁴M⁻¹s⁻¹; k_(d1) of 1.2 (±0.1)×10⁻²s⁻¹; k_(d2) of 3.2 (±0.8)×10⁻⁵s⁻¹; K_(A1) of 2.0×10⁷ M⁻¹; K_(A2) of 2.9×10⁹ M⁻¹.

[0066] Another embodiment of the present invention is a mutein that exhibits altered substrate specificity compared to its unmodified counterpart. A mutein exhibiting altered substrate specificity is a mutein that binds with increased affinity to a Fc domain of an antibody class or antibody species of a different type than that normally bound by its unmodified counterpart. In one embodiment, a mutein of a human FcεRIα protein with altered substrate specificity is a FcR that binds with increased affinity to a IgE antibody of another mammal, such as, but not limited to, a canine, feline, equine, murine, or rat IgE antibody. In another embodiment, a mutein of a human FcεRIα protein with altered substrate specificity is a FcR that binds with increased affinity to an antibody of another class, such as IgG, IgM, IgA, or IgD, with IgG being preferred. Such a mutein can also show altered species substrate specificity. Methods to determine whether a mutein exhibits altered substrate specificity are well known to those skilled in the art.

[0067] Yet another embodiment of the present invention is a mutein that exhibits increased solubility compared to its unmodified counterpart. Such a protein is less likely to form aggregates. Methods to determine whether a mutein exhibits increased solubility are well known to those skilled in the art.

[0068] As disclosed herein, the 3-D model representing a FcεRIα:Fc-Cε3/Cε4 complex is advantageous in determining strategies for producing muteins having an improved function, e.g., for identifying targets to modify in order to obtain muteins having improved functions. Examples of targets are as follows. A key feature of the human FcεRIα₁₋₁₇₆ protein is the crystal contacts in five space groups, a subset of which are predicted to interact directly with a Fc domain of an IgE antibody. Such contacts are included in the IgE binding domain which is unique for human FcεRIα in that the domain includes a tryptophan-containing hydrophobic ridge positioned on the top face of the crystal structure (i.e., amino acids W87, W10, W113, and W156 of SEQ ID NO:2) and an FG loop comprising amino acids from 155 to 158 of SEQ ID NO:2 that protrudes above the interface in an unusual manner. Particularly preferred amino acids are residues at positions of 85, 86, 87, and 110 of SEQ ID NO:2. Another key feature is the interface between domain 1 and domain 2 (i.e., the D1D2 interface) which includes amino acids 12, 13, 14, 15, 16, 17, 18, 20, 84, 85 and 86 in D1 and 87, 88, 89, 90, 91, 92, 93, 95, 104, 106, 108, 110, 111, 161, 163, 164, and 165 in D2 of SEQ ID NO:2. Also important are the two domains themselves: D1 includes amino acids 1 through 86 of SEQ ID NO:2; and D2 includes amino acids 87 through 176 of SEQ ID NO:2. Another important feature is the cleft between D1 and D2, which can be identified using the coordinates. Other areas of interest include the hydrophobic core which can be identified using the coordinates, the A′B loop of D1, which includes amino acids 18 and 19, the EF loop of D1, which includes amino acids 59-63, the BC loop of D2, which includes amino acids 110-114, the C strand of D2, which includes amino acids 114-123, the CC′ loop of D2, which includes amino acids 123-125, the C′E loop of D2, which includes amino acids 127-134, in the different confirmations observed in the five crystal forms, and the F strand of D2, which includes amino acids 147-155 of SEQ ID NO:2. Yet another striking feature is the finding that the amino and carboxyl termini of the human FcεRIα₁₋₁₇₆ protein are only 10 angstroms apart. Particularly preferred targets are a crystal contact cluster, a tryptophan-containing hydrophobic ridge, a FG loop in D2, a D1D2 interface, a cleft between D1 and D2, a domain 1, a domain 2, a hydrophobic core, a A′B loop of D1, a EF loop of D1, a BC loop of D2, a C strand of D2, a CC′ loop of D2, a C′E loop of D2, a strand of D2, the amino terminal five residues of said protein, and the carboxyl terminal five residues of said protein, with FcεRIα:Fc-Cε3/Cε4 interaction site 1, a FcεRIα:Fc-Cε3/Cε4 interaction site 2, a C strand of domain 2 of Fc8RIα, a C′E loop of domain 2 of FcεRIα, and a tryptophan-containing hydrophobic ridge of FcεRIα being particularly preferred. Preferred residues to target include residues at positions 85, 86, 87, 110, 113, 117, 119, 126,129,130, 131, 132,156, 157 and 158 of SEQ ID NO:2. In one embodiment, preferred regions to target are listed in Tables 3, 4, and 5. TABLE 3 Contact analysis between specified sets of atoms in FcεRIα:Fc-Cε3/Cε4 interaction site 1 set1 = ( segid A ) set2 = ( segid B ) definition of contact atoms: ( known and not hydrogen ) maximum distance cutoff between contact atoms: 4.0 List of contacting residue pairs between set1 and set2. The atoms that form the closest contact between the particular pair of residues and the corresponding distance are listed. atom in set 1 atom in set 2 distance (A) [ LYS 117 NZ ] [ GLY 335 O ] 3.24203 [ LYS 117 NZ ] [ ASP 362 OD2 ] 3.40928 [ ILE 119 CD1 ] [ ASN 394 O ] 2.99234 [ ALA 126 CB ] [ ARG 393 O ] 3.47281 [ ALA 126 CB ] [ ASN 394 C ] 3.8627 [ ALA 126 CB ] [ GLY 395 N ] 3.50267 [ TYR 129 OH ] [ ASP 362 O ] 2.80047 [ TYR 129 CE2 ] [ ALA 364 CB ] 3.81077 [ TRP 130 CZ2 ] [ ARG 334 NH2 ] 3.40032 [ TRP 130 CZ3 ] [ HIS 424 CE1 ] 3.908 [ TYR 131 CG ] [ ARG 334 CG ] 3.15693 [ TYR 131 CE2 ] [ VAL 336 CG2 ] 3.33025 [ TYR 131 CE2 ] [ ASP 362 O ] 3.72658 [ TYR 131 OH ] [ ALA 364 N ] 3.33849 [ TYR 131 OH ] [ HIS 424 ND1 ] 2.60229 [ GLU 132 OE1 ] [ ARG 334 NH1 ] 2.4186

[0069] TABLE 4 Contact analysis between specified sets of atoms in FcεRIα:Fc-Cε3/Cε4 interaction site 1 set1 = ( segid A ) set2 = ( segid D ) definition of contact atoms: ( known and not hydrogen ) maximum distance cutoff between contact atoms: 4.0 List of contacting residue pairs between set1 and set2. The atoms that form the closest contact between the particular pair of residues and the corresponding distance are listed. atom in set 1 atom in set 2 distance (A) [ SER 85 OG ] [ PRO 426 O ] 3.61996 [ SER 85 O ] [ ARG 427 CG ] 3.88945 [ ASP 86 O ] [ PRO 426 CB ] 3.23037 [ ASP 86 OD2 ] [ ARG 427 CD ] 3.37831 [ TRP 87 CH2 ] [ LEU 425 CD2 ] 3.4993 [ TRP 87 CZ2 ] [ PRO 426 CD ] 3.58257 [ TRP 87 NE1 ] [ ARG 427 N ] 3.96531 [ TRP 110 CG ] [ PRO 426 CG ] 3.30731 [ TRP 113 CH2 ] [ HIS 424 O ] 3.3407 [ TRP 156 CA ] [ PRO 333 O ] 3.71511 [ TRP 156 O ] [ ARG 334 CA ] 3.63918 [ TRP 156 O ] [ GLY 335 N ] 3.19027 [ GLN 157 NE2 ] [ CYS 329 N ] 3.96932 [ GLN 157 NE2 ] [ ASN 332 ND2 ] 2.70954 [ GLN 157 NE2 ] [ PRO 333 O ] 3.96239 [ GLN 157 OE1 ] [ ARG 334 NH1 ] 3.22424 [ LEU 158 CD1 ] [ GLY 335 O ] 3.71969 [ LEU 158 CD1 ] [ VAL 336 O ] 3.42542 [ MAN 246 O2 ] [ ARG 427 NH2 ] 3.54884

[0070] TABLE 3 Contact analysis between specified sets of atoms in FcεRIα-CHAPs interaction set1 = ( segid A ) set2 = ( segid E ) definition of contact atoms: ( known and not hydrogen ) maximum distance cutoff between contact atoms: 4.0 List of contacting residue pairs between set1 and set2. The atoms that form the closest contact between the particular pair of residues and the corresponding distance are listed. atom in set 1 atom in set 2 distance (A) [ ARG 111 NH1 ] [ CPS 101 O4 ] 3.46342 [ TRP 113 NE1 ] [ CPS 101 O4 ] 3.2081 [ TRP 113 CZ2 ] [ CPS 103 C16 ] 3.9932 [ TYR 116 CB ] [ CHA 102 O8 ] 3.23437 [ LYS 117 CD ] [ CHA 102 O6 ] 3.86424 [ LYS 154 CD ] [ CHA 102 O6 ] 3.11731 [ TRP 156 CZ2 ] [ CPS 103 C11 ] 3.36681 [ GLN 157 CG ] [ CHA 102 O7 ] 3.90519

[0071] In accordance with the present invention, a mutein having an improved function can be produced by a method that includes replacing at least one amino acid based on information derived from analyzing a 3-D model of the present invention to produce the mutein having the improved function. Knowledge of the structure of the extracellular domain of a human FcεRIα protein crystal, for example, permits the rational design and construction of modified forms of the protein by permitting the prediction and production of substitutions, insertions, deletions, inversions and/or derivatizations that effect an improved function. That is, analysis of 3-D models of the present invention provide information as to which amino acid residues are important and, as such, which amino acids can be changed without harming the protein. In making amino acid replacements, it is preferred to use amino acid replacements that have similar numbers of atoms and that allow conservation of salt bridges, hydrophobic interactions and hydrogen bonds unless the goal is to purposefully change such interactions. The 3-D structure of the human FcεRIα protein suggests that large deletions may not be desirable, particularly due to the relation between the various domains of the protein and the observation that most of the structure is well ordered in the crystal. An exception to this is the non-constrained loops of D1, which apparently could be deleted or shortened without harming the protein's function. These loops span amino acids 31-35 and 70-74 of SEQ ID NO:2.

[0072] It is to be appreciated that although one amino acid replacement capable of improving the function of a protein can substantially improve that function, more than one amino acid replacement can result in cumulative changes depending on the number and location of the replacements. For example, although one amino acid replacement capable of substantially increasing the stability of a protein can increase the melting temperature of that modified protein by about 1° C., about 5 to about 6 replacements may increase the melting temperature of the resultant protein by about 10° C.

[0073] In accordance with the present invention, the 3-D model of the complex has been analyzed, using techniques known to those skilled in the art, to determine the accessibility of the amino acids represented within the model to solvent. Such information is provided in, for example, Table 2.

[0074] A number of methods can be used to produce muteins of the present invention. One method includes the steps of: (a) analyzing a 3-D model substantially representing the coordinates specified in Table 1 to identify at least one amino acid of the modeled protein which if replaced by a specified amino acid would effect an improved function; and (b) replacing the identified amino acid(s) to produce a mutein having that improved function. In one embodiment, a method to produce a mutein includes the steps of (a) comparing a key region of a model of a human FcεRIα protein with the amino acid sequence of a FcR having an improved function compared to the unmodified FcεRIα protein in order to identify at least one amino acid segment of the FcR with the improved function that if incorporated into the FcεRIα protein represented by the model would give the FcεRIα protein the improved function; and (b) incorporating the segment into the FcεRIα protein, thereby providing a mutein with the improved function. In another embodiment, a method to produce a protein includes the steps of: (a) using a model representing a human FcεRIα protein to identify a 3-D arrangement of residues that can be randomized by mutagenesis to allow the construction of a library of molecules from which a improved function can be selected; and (b) identifying at least one member of the mutagenized library having the improved function. In one example, a mutein is produced by a method that includes the steps of: (a) effecting random mutagenesis of nucleic acid molecules encoding a target of a FcεRIα protein as identified by analyzing a model of that protein, such as an IgE binding domain; (b) cloning such mutagenized nucleic acid molecules into a phage display library, wherein said phage display library expresses the target; and (c) identifying at least one member of the library that expresses a target with an improved function, such as an antibody binding domain exhibiting increased affinity for an antibody. As stated above, the model allows the use of this technique in a straightforward manner that could not be accomplished in the absence of the model. It is to be also noted that these methods can also be used with other models of the present invention to produce muteins of the present invention.

[0075] The present invention includes a number of methods, based on analysis of a 3-D model of the present invention, to replace (i.e., add, delete, substitute, invert, derivatize) at least one amino acid residue in the protein represented by the model in order to produce a mutein of the present invention. Such methods include, but are not limited to: (a) replacing at least one amino acid in at least one non-constrained loop of domain 1 in an area proximal to the FceRI gamma chain putative binding site; (b) joining an amino-terminal amino acid residue to a carboxyl-terminal amino acid residue of an extracellular domain of a FcεRIα protein; (c) replacing at least one amino acid site with an amino acid suitable for derivatization; (d) replacing at least one pair of amino acids of the protein with a cysteine pair to enable the formation of a disulfide bond that stabilizes the protein; (e) removing at least a portion of the region between the B strand and C strand of domain 1; (f) removing at least a portion of the region between the C strand and E strand of domain 1; (g) replacing at least one amino acid in the IgE binding domain in order to increase the affinity between an IgE antibody and the protein; (h) replacing at least one amino acid of the protein with an amino acid such that the replacement decreases the entropy of unfolding of the protein; (i) replacing at least one asparagine or glutamine of the protein with an amino acid that is less susceptible to deamidation than is the amino acid to be replaced; (j) replacing at least one methionine, histidine or tryptophan with an amino acid that is less susceptible to an oxidation or reduction reaction than is the amino acid to be replaced; (k) replacing at least one arginine of the protein with an amino acid that is less susceptible to dicarbonyl compound modification than is the amino acid to be replaced; (l) replacing at least one amino acid of the protein susceptible to reaction with a reducing sugar sufficient to reduce protein function with an amino acid less susceptible to that reaction; (m) replacing at least one amino acid of the protein with an amino acid capable of increasing the stability of the inner core of the protein; (n) replacing at least one amino acid of the protein with at least one N-linked glycosylation site; (o) replacing at least one N-linked glycosylation site of the protein with at least one amino acid that does not comprise an N-linked glycosylation site; and (p) replacing at least one amino acid of the protein with an amino acid that reduces aggregation of the protein.

[0076] Amino acid replacements can be carried out using recombinant DNA techniques known to those skilled in the art, including site-directed mutagenesis (e.g., oligonucleotide mutagenesis, random mutagenesis, polymerase chain reaction (PCR)-aided mutagenesis, gapped-circle site-directed mutagenesis) or chemical synthetic methods of a nucleic acid molecule encoding the desired protein, such as, but not limited to a human FcεRIα protein, followed by expression of the mutated gene in a suitable expression system, preferably an insect, mammalian, bacterial, yeast, insect, or mammalian expression system. See, for example, Sambrook et al., ibid.

[0077] One embodiment of the present invention is a mutein in which at least one amino acid in at least one non-constrained loop of a FcεRIα protein is replaced in order to improve a function of the protein. Finding that the human FcεRIα protein had such loops was surprising, and it is believed, without being bound by theory, that a mutein in which at least a portion of at least one such loop is replaced, would at least exhibit enhanced stability. In a preferred embodiment, at least a portion of one or more of such loops is (are) deleted. Preferred loops to replace are in domain 1 (i.e., spanning amino acids 31-35 and 70-74 of SEQ ID NO:2), preferably in an area proximal to the FceRI gamma chain putative binding site, i.e., the site on the FcεRIα protein to which the gamma chain of the high affinity Fc epsilon receptor is thought to bind. In a preferred embodiment, one or more amino acids is replaced to make loops shorter, but including 1 or 2 hydrophobic residues to pack toward the protein interior and at least one hydrophilic residue to maintain solubility.

[0078] Another embodiment of the present invention is a mutein of the extracellular domain of a FcεRIα protein in which an N-terminal (amino-terminal) amino acid residue is joined, preferably covalently, to a C-terminal (carboxyl-terminal) amino acid residue in order to improve a function of the protein. Finding that the N-termini and C-termini of the human FcεRIα protein were only 10 angstroms apart was quite surprising. Without being bound by theory, it is believed that such a mutein would at least exhibit enhanced stability. Furthermore, a covalent linker used to join the termini could also include a substance useful, for example, to anchor a mutein on a surface, as would be useful, for example, in a diagnostic assay, or to label the mutein. For a protein consisting of SEQ ID NO:2, a preferred N-terminal residue is an amino acid residue at position 1, 2, or 3 of SEQ ID NO:2, and a preferred C-terminal residue is an amino acid residue at position 174, 175, or 176 of SEQ ID NO:2. Covalent linkage can be accomplished by methods known to those skilled in the art, such as, but not limited to, adding one or more N-terminal and C-terminal cysteines and crosslinking them with chemical compounds, adding additional residues in the coding sequence to allow the formation of a disulfide bond, or adding one or more lysines and coupling them through a 10 angstrom linker, and including non-natural amino acid analogues by synthetic methods or by a combination of biosynthetic and organosynthetic methods. Examples of a substance to add to a covalent linker includes: ligands useful in allowing for the attachment of a mutein to a surface, such as biotin and related compounds, avidin and related compounds, metal binding compounds, sugar binding compounds, immunoglobulin binding domains, and other tag domains; and detectable markers, such as enzyme labels, physical labels, radioactive labels, fluorescent labels, chemiluminescent labels, and chromophoric labels. Examples include, but are not limited to, alkaline phosphatase, horseradish peroxidase, digoxygenin, luciferase, other light-generating enzymes and magnetic beads. It is also to be noted that ligands can function as detectable markers.

[0079] Another embodiment of the present invention is a mutein in which at least one amino acid is replaced with an amino acid suitable for derivatization. Muteins in which at least one amino acid is replaced with an amino acid suitable for derivatization include proteins that are chemically modified (e.g., a lysine already existing on the protein is modified) as well as those in which an amino acid residue is replaced with a different amino acid residue (e.g., a glycine with a lysine) as well as proteins to which a substance is added, preferably to the amino or carboxyl terminus of the protein. Examples of such substances include ligands and detectable markers as disclosed above. Preferable amino acids to replace include residues that are solvent exposed (e.g., those listed in Table 2), but that are preferably not within about 10 angstroms of the IgE binding domain. In one embodiment, a glycosylation site, or other solvent exposed site, is replaced with a charged or polar residue to increase solubility or create more stable muteins. Glycosylation sites in human FcεRIα. protein include amino acids 21, 42, 50 74, 135, 140, and 166 of SEQ ID NO:2. A preferred amino acid to use as a replacement, or to chemically modify directly, includes a cysteine or a lysine, with a cysteine being preferred. Compounds to use in chemical derivatizations are known to those skilled in the art; cysteines can, for example, be derivatized with maleimides.

[0080] Another embodiment of the present invention is a mutein in which a pair of amino acids have been replaced with a cysteine pair in order to improve the function of the mutein, at least by increasing stability. Cysteine pairs can be substituted into a FcεRIα protein at any two residue positions identified with available programs and algorithms that would allow the formation of an undistorted disulfide bridge. In one embodiment, a serine and lysine near the termini of the protein is each replaced with a cysteine. In another embodiment, cysteine pairs are replaced with other amino acids, such as serines to eliminate non-essential disulfide bonds.

[0081] Another embodiment of the present invention is a mutein in which at least one amino acid is replaced in the region between the B strand and C strand of domain 1 and/or the region between the C and E strand of domain 1. In a preferred embodiment, at least a portion of such a region is deleted.

[0082] Another embodiment of the present invention is a mutein in which at least one amino acid is replaced in the IgE binding domain in order to increase the affinity between an IgE antibody and the protein. Preferred residues to replace are in or near the IgE binding domain, or IgE binding site, as determined by analysis of the 3-D model. Such residues are preferably within about 10 angstroms of residues identified by mutagenesis and further shown by model to be in an IgE binding site. Examples of such residues include amino acids 87, 110, 113, 115, 117, 118, 120, 121, 122, 123, 128, 129, 131, 149, 153, 154, 155, 156, 157, 158, and 159 of SEQ ID NO:2, and amino acids within 10 angstroms of such listed amino acids. In one embodiment, preferred amino acids to replace include amino acids 87, 115, 117, 118, 120-123, 128, 129, 131, 149, 153, 155 and 159 of SEQ ID NO:2 as well as any surface residue within about 10 angstroms of any of the listed amino acids, with amino acids 87, 117, 121, 123, 128, 159 of SEQ ID NO:2 or SEQ ID NO:4 as well as any surface residue within about 10 angstroms of amino acids 87, 117, 121, 123, 128, 159 of SEQ ID NO:2 being particularly preferred. It is to be noted that amino acids 115, 118, 120, 131, 149 and 155 of SEQ ID NO:2 are buried, and that amino acids that are partially buried or glycine include residues 122, 129 and 153. Additional amino acid residues to target include those in the A′B loop of D1, and EF loop of D1. Note that these residues are not the same as those shown in mutation studies to affect IgE binding since some of those mutants have mutations in amino acids that are internal to the protein; this finding can only be made by analysis of a model of the present invention.

[0083] Another embodiment of the present invention is a mutein in which at least one amino acid is replaced with an amino acid capable of increasing the stability of the inner core or surface of the protein. Preferred amino acids to replace are hydrophilic residues located in the hydrophobic core of the protein and/or hydrophobic amino acids at the protein surface that are not within about 10 angstroms of the IgE binding domain residues of D1 or D2. Preferred amino acids to replace into the hydrophobic core are hydrophobic residues such as, but not limited to, tryptophan, leucine, isoleucine, valine and alanine, as well as space filling amino acids, such as other aromatic amino acids. Preferred amino acids to replace onto the surface are polar amino acids, such as, but not limited to, glutamic acid, glutamine, aspartic acid, asparagine, histidine and serine. Muteins having one or more such amino acid replacements would exhibit at least increased stability and/or reduced aggregation. Additional preferred amino acid replacements are those that introduce salt bridges at the protein surface to stabilize protein folds. It is noted that the cysteines at positions 26 and 68 of SEQ ID NO:2 form a disulfide bond in domain 1 that is somewhat exposed to solvent, depending especially on the conformation of the Dl “30 loop” (i.e., amino acids 31-35 of SEQ ID NO:2). In one embodiment, changes in neighboring residues can be made in, for example, residues 1-5, 27-37, 49-52, or 69-75, to bury this disulfide from exposure to solvent. For example, phage display of receptors with randomized mutations in the 30 loop, might be useful for selecting receptors that react less well with reducing reagents and have a more stable D1 core.

[0084] Another embodiment of the present invention is a mutein in which at least one amino acid is replaced with an amino acid that decreases the entropy of unfolding of the protein. The entropy of unfolding of a protein can be measured and compared to that of another protein using techniques known to those skilled in the art. A number of methods known to those skilled in the art can be used to reduce the number of protein conformations possible in the unfolded state, thereby improving the ability of the protein to fold correctly. One embodiment of the present invention for decreasing the entropy of unfolding includes replacing at least one amino acid of the protein with a specified amino acid in order to maintain certain desirable phi and psi backbone conformation angles in the protein; see, for example, PCT International Publication No. WO 89/01520, by Drummond et al., published Feb. 23, 1989. For example, a proline residue in a protein constrains the backbone conformation to certain restricted angles. Analysis of a 3-D model of a protein of the present invention permits the identification of candidate replacement positions in the protein that have the conformation expected for a proline, but that do not have a proline in them. Such knowledge is used to introduce prolines into such candidate replacement positions to “anchor” the resultant mutein in the desired conformation. The 3-D model also permits the identification of candidate replacement sites that if replaced with a proline do not substantially disrupt the 3-D structure of the resultant protein. Similarly, glycines in appropriate positions can be replaced with an amino acid having a β carbon atom or a branched carbon atom, preferably an alanine, in order to stabilize the backbone of the protein.

[0085] Another embodiment of the present invention is a mutein in which at least one asparagine or glutamine is replaced with an amino acid that is less susceptible to deamidation. Preferred amino acids to replace include solvent accessible asparagines and glutamines.

[0086] Another embodiment of the present invention is a mutein in which at least one methionine, histidine or tryptophan is replaced with an amino acid that is less susceptible to an oxidation or reduction reaction. Preferred amino acids to replace include M98, H70, and H41. It would not be preferred to replace any of the tryptophans, nor H108 or H134 of SEQ ID NO:2.

[0087] Another embodiment of the present invention is a mutein in which at least one arginine is replaced with an amino acid that is less susceptible to dicarbonyl compound modification. Although R174 could be changed, it would probably not be preferable to change amino acids at the D1D2 interface or near the IgE binding site, such as amino acids 15, 106, or 111 of SEQ ID NO:2.

[0088] Another embodiment of the present invention is a mutein in which at least one amino acid that is susceptible to reaction with a reducing sugar sufficient to reduce protein function is replaced with an amino acid that is less susceptible to such a reaction. For example, lysines, glutamines and asparagines that could react with a sugar, such as galactose, glucose or lactose can be replaced with non-reactive amino acids.

[0089] Another embodiment of the present invention is a mutein in which one or more N-linked glycosylation sites are added to or removed from the protein, preferably by substitution with an appropriate amino acid. A FcεRIα protein with additional N-linked glycosylation sites is more soluble. The ability to design a FcεRIα protein having fewer, or no, N-linked glycosylation sites is also valuable as production of such a protein from production run to production run is likely to be more uniform. One embodiment is a FcεRIα mutein with no N-linked glycosylation sites that is stable, active, and soluble. Such a protein has an advantage of being produced in E. coli at low cost. In one embodiment, one or more exposed hydrophobic amino acids are changed to charged residues that form salt bridges to stabilize the protein fold and make it soluble. It is to be noted that the glycosylation sites that appear to be most often observed in the different crystal structures in the same conformation are the carbohydrate attached to positions 42 and 166 of SEQ ID NO:2. The carbohydrate attached to position 42 always appears to cover the phenylalanine at position 60 of SEQ ID NO:2. As such, one embodiment of the present invention is to remove the glycosylation site at position 42, e.g., by substitution with a suitable amino acid. This embodiment has the additional advantage that the resultant mutein has an exposed phenylalanine at position 60, thereby leading to increased IgE binding activity.

[0090] Another embodiment of the present invention is a mutein in which at least one amino acid is replaced with an amino acid that reduces aggregation and increases solubility of the protein, such as, for example, replacing one or more hydrophobic residues on the surface with one or more hydrophilic residues. Other examples of such amino acids to replace are disclosed herein.

[0091] Another embodiment of the present invention to enhance stability is the addition of polyethylene glycol (PEG) groups to a FcR protein, i.e., to produce a “pegylated” FcR protein. In one embodiment, the PEG group(s) can substitute for carbohydrate group(s) due to removal of one or more N-glycosylation sites. Such PEG group(s) can be attached to easily modifiable residues, such as cysteines or lysines, on the surface of the protein, such residues identifiable by analysis of a 3-D model of the present invention.

[0092] Another embodiment of the present invention is a mutein that comprises a FcR having a substance, such as a ligand or detectable marker, attached to an amino acid of the protein such that the substance does not substantially interfere with the antibody binding activity of the protein. The substance is attached in such a manner that the substance is also capable of performing its function, such as binding to a second member of a ligand pair or enabling detection of the protein. The FcR to which a substance is attached can be either an unmodified protein or a mutein of the present invention. Suitable attachment sites can be identified using 3-D models of the present invention. Preferred attachment sites include solvent exposed amino acids, such as those listed in Table 2. Substances can be attached, or conjugated, to the protein using techniques known to those skilled in the art. It is to be appreciated that a preferred method to attach a substance to an amino acid is to modify that amino acid to have a reactive attachment site, such as is present on cysteine and lysine amino acids. As such, an attachment site comprising a solvent exposed amino acid refers to the nature of the amino acid prior to any modification required for attachment. Examples of suitable substances to attach to a FcR include any compound capable of binding to or reacting with another substance, such as those described for attachment to a covalent linker.

[0093] It is to be appreciated that muteins of the present invention can include amino acids which are not modified because they would negatively impact the function of the protein. Such amino acids can be identified using a 3-D model of the present invention.

[0094] It should also be appreciated that it is within the scope of the present invention to expand the use of models of the present invention to produce models of and make modifications to any suitable FcRs or other Ig domain-containing proteins to produce muteins having a desired function.

[0095] The present invention also includes a mutein that binds to an IgE binding domain of a FcεRIα protein, wherein the mutein has an improved function compared to a Fc-Cε3/Cε4 protein comprising amino acid sequence SEQ ID NO:6. Such an improved function can include increased stability compared to the stability of a human IgE Fc region comprising amino acid sequence SEQ ID NO:6, increased affinity for a FcεRIα protein compared to the FcεRIα affinity of a human IgE Fc region comprising amino acid sequence SEQ ID NO:6, altered substrate affinity compared to the affinity for human FcεRIα of a human IgE Fc region comprising amino acid sequence SEQ ID NO:6, and increased solubility compared to the solubility of a human IgE Fc region comprising amino acid sequence SEQ ID NO:6. Such a mutein is produced by a method that includes the steps of (a) analyzing a three-dimensional model substantially representing the atomic coordinates specified in Table 1 to identify at least one amino acid of the Fc-Cε3/Cε4 protein represented by said model which if replaced by a specified amino acid would effect said improved function of said Fc-Cε3/Cε4 protein; and (b) replacing said identified amino acid(s) to produce said mutein having said improved function. Fc muteins can be identified and produced in a manner similar to that described herein for FcR muteins. Antibody muteins have a variety of uses, including but not limited to, diagnostic and therapeutic uses. For example, muteins could be used to image cells that express an antibody receptor protein, such as NMR-specific labeling for in vivo imaging to detect, for example, mast cell cancers, asthma, and other pathologies, or to treat cancers that express an antibody receptor protein using, for example, radioimmune therapy of derivatized IgE. Muteins could also be used for monitoring FcR expression in atopic individuals (e.g. with a tag for one-step FACS analysis) or for monitoring IgE in atopic individuals. Muteins could also be used as inhibitors or as toxin-IgE-Fc fusion proteins to target FcR-expressing cells to kill them (e.g. in mast cell tumors or severe allergy). Also muteins that affect the low affinity affinity IgE-receptor (FceRII) binding but not FceRI binding could be designed or selected.

[0096] The present invention also includes nucleic acid molecules that encode muteins of the present invention as well as recombinant molecules and recombinant cells that include such nucleic acid molecules. Methods to produce such proteins are also disclosed herein.

[0097] The present invention also includes the following novel structures as identified by a 3-D model of the present invention. Preferred structures exhibiting direct interaction between IgE and FcεRIα include FcεRIα:Fc-Cε3/Cε4 interaction site 1, a FcεRIα:Fc-Cε3/Cε4 interaction site 2, a C strand of domain 2 of FcεRIα, a C′E loop of domain 2 of FcεRIα, and a tryptophan-containing hydrophobic ridge of FcεRIα. Other preferred structures include a crystal contact cluster involved in IgE binding; a FG loop in D2; a D1D2 interface; a cleft between D1 and D2; a domain 1; a domain 2; a hydrophobic core; a A′B loop of D1; a EF loop of D1; a BC loop of D2; a CC′ loop of D2; and a strand of D2. Particularly preferred are (a) a FcεRIα:Fc-Cε3/Cε4 interaction site 1 pocket comprising an amino acid residue at position 131 of SEQ ID NO:2 and amino acid residues at positions 9, 11, 37, 39, and 99 of SEQ ID NO:6 and (b) a FcεRIα:Fc-Cε3/Cε4 interaction site 2 pocket comprising amino acid residues at positions 85, 86, 87, and 110 of SEQ ID NO:2 and amino acid residue at position 101 of SEQ ID NO:6. Also included herein are nucleic acid molecules to encode such structures as well as recombinant molecules and recombinant cells that include such nucleic acid molecules. Also included are methods to produce such structures and models thereof.

[0098] The present invention also includes isolated nucleic acid molecules encoding proteins of the present invention, including, but not limited to, unmodified proteins, novel structures within such proteins, and muteins. As used herein, an isolated nucleic acid molecule encoding a protein is a nucleic acid molecule that has been removed from its natural milieu. As such, “isolated” does not reflect the extent to which the nucleic acid molecule has been purified. An isolated nucleic acid molecule can be DNA, RNA, or derivatives of either DNA or RNA.

[0099] A nucleic acid molecule encoding a mutein of the present invention can be produced by mutation of parental protein genes (e.g., unmodified or previously modified protein-encoding genes, or portions thereof) using recombinant DNA techniques heretofore disclosed or by chemical synthesis. Resultant mutein nucleic acid molecules can be amplified using recombinant DNA techniques known to those skilled in the art, such as PCR amplification or cloning (see, for example, Sambrook et al., ibid.), or by chemical synthesis. A mutein can also be produced by chemical modification of a protein expressed by a nucleic acid molecule encoding an unmodified protein or mutein-encoding gene.

[0100] Proteins of the present invention can be produced in a variety of ways, including production and recovery of recombinant proteins and chemical synthesis. In one embodiment, a protein of the present invention is produced by culturing a cell capable of expressing the protein under conditions effective to produce the protein, and recovering the protein. A preferred cell to culture is a recombinant cell that is capable of expressing the protein, the recombinant cell being produced by transforming a host cell with one or more nucleic acid molecules of the present invention. Transformation of a nucleic acid molecule into a host cell can be accomplished by any method by which a nucleic acid molecule can be inserted into a cell. Transformation techniques include, but are not limited to, transfection, electroporation, microinjection, lipofection, adsorption, and protoplast fusion. A recombinant cell may remain unicellular or may grow into a tissue, organ or a multicellular organism. Transformed nucleic acid molecules of the present invention can remain extrachromosomal or can integrate into one or more sites within a chromosome of a host cell in such a manner that their ability to be expressed is retained.

[0101] Suitable host cells to transform include any cell that can be transformed. Host cells can be either untransformed cells or cells that are already transformed with at least one nucleic acid molecule. Host cells of the present invention can be endogenously (i.e., naturally) capable of producing a protein of the present invention, but such cells are not preferred. Host cells of the present invention can be any cell that when transformed with a nucleic acid molecule of the present invention are capable of producing a protein of the present invention, including bacterial, yeast, other fungal, insect, animal, and plant cells. Preferred host cells include bacterial, yeast, insect and mammalian cells, and more preferred host cells include Escherichia, Bacillus, Saccharomyces, Pichia, Trichoplusia, Spodoptera and mammalian cells. Particularly preferred host cells are Trichoplusia ni cells and Spodoptera frugiperda cells with T. ni cells being particularly preferred.

[0102] A recombinant cell is preferably produced by transforming a host cell with a recombinant molecule comprising a nucleic acid molecule of the present invention operatively linked to an expression vector containing one or more transcription control sequences. The phrase operatively linked refers to insertion of a nucleic acid molecule into an expression vector in a manner such that the molecule is able to be expressed when transformed into a host cell. As used herein, an expression vector is a DNA or RNA vector that is capable of transforming a host cell, of replicating within the host cell, and of effecting expression of a specified nucleic acid molecule. Expression vectors can be either prokaryotic or eukaryotic, and are typically viruses or plasmids. Expression vectors of the present invention include any vectors that function (i.e., direct gene expression) in recombinant cells of the present invention, including in bacterial, yeast, other fungal, insect, animal, and plant cells. Preferred expression vectors of the present invention can direct gene expression in bacterial, yeast, insect and mammalian cells.

[0103] Nucleic acid molecules of the present invention can be operatively linked to expression vectors containing regulatory control sequences such as promoters, operators, repressors, enhancers, termination sequences, origins of replication, and other regulatory control sequences that are compatible with the host cell and that control the expression of the nucleic acid molecules. In particular, recombinant molecules of the present invention include transcription control sequences. Transcription control sequences are sequences which control the initiation, elongation, and termination of transcription. Particularly important transcription control sequences are those which control transcription initiation, such as promoter, enhancer, operator and repressor sequences. Suitable transcription control sequences include any transcription control sequence that can function in at least one of the recombinant cells of the present invention. A variety of such transcription control sequences are known to those skilled in the art. Preferred transcription control sequences include those which function in bacterial, yeast, insect and mammalian cells.

[0104] It may be appreciated by one skilled in the art that use of recombinant DNA technologies can improve expression of transformed nucleic acid molecules by manipulating, for example, the number of copies of the nucleic acid molecules within a host cell, the efficiency with which those nucleic acid molecules are transcribed, the efficiency with which the resultant transcripts are translated, and the efficiency of post-translational modifications. Recombinant techniques useful for increasing the expression of nucleic acid molecules of the present invention include, but are not limited to, operatively linking nucleic acid molecules to high-copy number plasmids, integration of the nucleic acid molecules into one or more host cell chromosomes, addition of vector stability sequences to plasmids, substitutions or modifications of transcription control signals (e.g., promoters, operators, enhancers), substitutions or modifications of translational control signals (e.g., ribosome binding sites, Shine-Dalgamo sequences), modification of nucleic acid molecules of the present invention to correspond to the codon usage of the host cell, deletion of sequences that destabilize transcripts, and use of control signals that temporally separate recombinant cell growth from recombinant protein production during fermentation. The activity of an expressed recombinant protein of the present invention may be improved by fragmenting, modifying, or derivatizing nucleic acid molecules encoding such a protein.

[0105] In accordance with the present invention, recombinant cells can be used to produce proteins by culturing such cells under conditions effective to produce such a protein, and recovering the protein. Effective conditions to produce a protein include, but are not limited to, appropriate media, bioreactor, temperature, pH and oxygen conditions that permit protein production. An appropriate medium refers to any medium in which a cell of the present invention, when cultured, is capable of producing the protein. An effective medium is typically an aqueous medium comprising assimilable carbohydrate, nitrogen and phosphate sources, as well as appropriate salts, minerals, metals and other nutrients, such as vitamins. The medium may comprise complex nutrients or may be a defined minimal medium. Cells of the present invention can be cultured in conventional fermentation bioreactors, which include, but are not limited to, batch, fed-batch, cell recycle, and continuous fermentors. Culturing can also be conducted in shake flasks, test tubes, microtiter dishes, and petri plates. Culturing is carried out at a temperature, pH and oxygen content appropriate for the recombinant cell. Such culturing conditions are well within the expertise of one of ordinary skill in the art.

[0106] Depending on the vector and host system used for production, resultant proteins may either remain within the recombinant cell; be secreted into the fermentation medium; be secreted into a space between two cellular membranes, such as the periplasmic space in E. coli; or be retained on the outer surface of a cell or viral membrane. The phrase “recovering the protein” refers simply to collecting the whole fermentation medium containing the protein and need not imply additional steps of separation or purification. Proteins of the present invention can be purified using a variety of standard protein purification techniques, such as, but not limited to, affinity chromatography, ion exchange chromatography, filtration, electrophoresis, hydrophobic interaction chromatography, gel filtration chromatography, reverse phase chromatography, chromatofocusing and differential solubilization.

[0107] The present invention also includes isolated (i.e., removed from their natural milieu) antibodies that selectively bind to a FcR or antibody of the present invention. As used herein, the term “selectively binds to” refers to the ability of antibodies of the present invention to preferentially bind to specified proteins of the present invention. Binding can be measured using a variety of methods standard in the art including enzyme immunoassays (e.g., ELISA), immunoblot assays, etc.; see, for example, Sambrook et al., ibid. Isolated antibodies of the present invention can include antibodies in a bodily fluid (such as, but not limited to, serum), or antibodies that have been purified to varying degrees. Antibodies of the present invention can be polyclonal or monoclonal. Functional equivalents of such antibodies, such as antibody fragments and genetically-engineered antibodies (including single chain antibodies or chimeric antibodies that can bind to more than one epitope) are also included in the present invention. Antibodies can be produced using methods known to those skilled in the art. A preferred method to produce antibodies of the present invention includes (a) administering to an animal an effective amount of a protein of the present invention to produce the antibodies and (b) recovering the antibodies. In another method, antibodies of the present invention are produced recombinantly using techniques as heretofore disclosed to produce proteins of the present invention. Antibodies raised against defined proteins can be advantageous because such antibodies are not substantially contaminated with antibodies against other substances that might otherwise cause interference in a diagnostic assay or side effects if used in a therapeutic composition.

[0108] Antibodies of the present invention have a variety of potential uses that are within the scope of the present invention. Examples of such uses are disclosed in WO 98/27208, ibid., see, for example, page 24; such uses are incorporated by reference herein in their entireties.

[0109] A FcR of the present invention can include chimeric molecules comprising at least a portion of a FcR that binds to an antibody and a second molecule that enables the chimeric molecule to be bound to a substrate in such a manner that the antibody receptor portion binds to the antibody in at least as effective a manner as a FcR that is not bound to a substrate. An example of a suitable second molecule includes a portion of an immunoglobulin molecule or another ligand that has a suitable binding partner that can be immobilized on a substrate, e.g., biotin and avidin, or a metal-binding protein and a metal (e.g., His), or a sugar-binding protein and a sugar (e.g., maltose). An antibody of the present invention can also be part of a chimeric molecule.

[0110] The present invention includes uses of proteins, antibodies and inhibitory compounds of the present invention for the diagnosis and treatment of allergy and the regulation of other immune responses in an animal.

[0111] One embodiment is a therapeutic composition comprising at least one of the following therapeutic compounds: an inhibitory compound of the present invention, a mutein of the present invention, or an antibody of the present invention. Also included is a method to protect an animal from allergy or other abnormal immune responses. Such a method includes the step of administering a therapeutic composition of the present invention to the animal. As used herein, the ability of a therapeutic composition of the present invention to protect an animal from allergy or other abnormal immune responses refers to the ability of that composition to, for example, treat, ameliorate or prevent allergy or other abnormal immune responses. General characteristics of therapeutic compositions and methods to produce and use such therapeutic compositions are disclosed, for example, in WO 98/27208, ibid., see, for example, page 39-47; such compositions and methods are incorporated by reference herein in their entireties. It is to be noted that although the compositions and methods disclosed in WO 98/27208, ibid., relate to feline FcεRIα proteins, they are also applicable to therapeutic compositions of the present invention. Therapeutic compositions of the present invention are advantageous because they can be derived from analysis of 3-D models of the present invention and have improved functions, such as efficacy and safety.

[0112] Another embodiment is a diagnostic reagent comprising a mutein of the present invention. As used herein, a diagnostic reagent is a composition that includes a mutein that is used to detect allergy or other abnormal immune responses in an animal. Also included in the present invention are methods, including in vivo methods and in vitro methods, to (a) detect allergy or other abnormal immune response, or susceptibility thereto, in an animal, comprising use of a diagnostic reagent comprising a mutein of the present invention and (b) to enhance the performance of an IgE binding assay, said method comprising incorporating into the assay a mutein of the present invention. General characteristics of diagnostic reagents and methods to produce and use such diagnostic reagents are disclosed, for example, in WO 98/27208, ibid., see, for example, page 2-39; such reagents and methods are incorporated by reference herein in their entireties. It is to be noted that although the reagents and methods disclosed in WO 98/27208, ibid., relate to feline FcεRIα proteins, they are also applicable to diagnostic reagents, kits and detection methods of the present invention. Muteins of the present invention are advantageous in such applications because of their enhanced affinity for antibodies, altered specificity, enhanced solubility and/or enhanced stability, enabling for example use in otherwise adverse conditions and longer shelf-life.

[0113] The following examples are provided for the purposes of illustration and are not intended to limit the scope of the invention.

EXAMPLE

[0114] This Example describes the production and analysis of a crystal and model of the present invention. It is to be noted that numbering of Fc-Cε3/Cε4 residues follows the convention of Dorrington et al, ibid.

[0115] The initiation of IgE-mediated allergic responses requires the binding of IgE antibody to its high affinity receptor, FcεRI. Crosslinking of FcεRI initiates an intracellular signal transduction cascade that triggers the release of mediators of the allergic response. The interaction of IgE-Fc domains with FcεRI is a key recognition event that is central to this process and mediated by the extracellular domains of the α-chain of FcεRI. This Example describes the solution of a crystal structure of the human IgE-Fc:FcεRIα complex, the coordinates of which are disclosed in Table 1. The crystal structure reveals that one receptor binds one IgE-Fc asymmetrically through interactions at two sites involving both N-terminal IgE-Fc Cε3 domains. The interaction of one receptor with IgE-Fc blocks the high-affinity binding of a second receptor and features of this interaction are conserved in other Fc receptor family members. The structural analysis suggests new approaches to the inhibition of IgE binding to FcεRI for the treatment of allergy and asthma.

[0116] A. Introduction

[0117] The high affinity IgE receptor (FcεRI) is found on the surface of effector cells of the immune system that initiate cellular reactions associated with the allergic response, anaphylaxis and anti-parasitic immunity^(1,2). The human receptor can form either a trimeric αγ₂ or tetrameric αβγ₂ structure on cell surfaces, with the extracellular domains of the α-chain conferring the ability to bind antibodies of the IgE class with high affinity (K_(D)˜10⁻⁹-10⁻¹⁰M). IgE antibodies bind to the receptor in the absence of antigen and thus the receptor adopts the antigenic specificity of the prevalent IgE repertoire. Crosslinking of the receptor through the engagement of antigen:antibody interactions leads to the initiation of a lyn and syk kinase-mediated signal transduction cascade, analogous to that induced by T and B cell receptors³⁻⁵. In mast cells, receptor activation leads to rapid degranulation and release of histamine followed by the synthesis and release of prostaglandins, leukotrienes, cytokines and other mediators of the allergic response. Anti-parasitic responses can be triggered through a similar activation of eosinophils, leading to the release of granular proteins toxic to schistosomes and other parasites. FcβRI belongs to a family of antibody-binding receptors that also mediate interactions of soluble IgG and IgA antibodies with cells of the immune system^(3,5). IgG-Fc receptors regulate inflammation pathways, B cell development, and Natural Killer Cell activation and are therefore important in many aspects of immunity and disease.

[0118] Atopic diseases, such as allergy, asthma, and eczema, comprise a wide spectrum of pathologies associated with the inappropriate activation of the immune system to environmental antigens^(6,7). Dramatic increases in atopic disease have been observed in this century, particularly in developed countries. Allergic diseases have been associated with the IgE network through genetic studies in both mice and humans, suggesting a role for polymorphisms of the FcεRI β-chain and CD14 in atopic individuals^(7,8). The interaction of the IgE antibody with FcεRI is central to these immune reactions, providing an attractive target for the inhibition of all IgE-mediated allergic disease. Clinical studies of allergic individuals using anti-IgE monoclonal antibody therapy has demonstrated that this is a viable approach to disease treatment^(9,10). Further development of treatments for allergy, asthma and anaphylaxis, may benefit from structural insights into the IgE:FcεRI interaction.

[0119] A recent report disclosed the crystal structure of the human FcεRI α-chain ectodomains¹¹, which revealed a highly bent arrangement of two immunoglobulin domains. Four solvent-exposed tryptophans cluster at the top of the receptor, forming a large hydrophobic surface for potential interactions with the IgE-Fc. This tryptophan cluster borders the Fc binding-site mapped by mutagenesis studies, which implicate residues in the second domain of the receptor in IgE binding. The structural and functional data suggested that a large convex surface of the receptor could be involved in binding IgE, raising questions about the role of the tryptophans, the convex nature of the binding site and the mechanisms underlying the stoichiometry and binding specificity with IgE.

[0120] These questions are addressed with the solution of a crystal structure of a complex of the human IgE-Fc with FcεRI as disclosed herein as well as of a crystal structure of the unbound IgE-Fc fragment as disclosed in 60/189,403, ibid. The structure of the complex reveals two interaction sites for the IgE-Fc on the receptor surface and clarifies how a 1:1 complex between antibody and receptor is formed. The two IgE-Fc Cε3 domains bind to distinct sites on the receptor; one is formed by the C-C′ loop in the receptor D2 domain, while the second site involves the four solvent-exposed tryptophans. The IgE Cε4 domains do not form direct contacts with the receptor and point away from the Cε3 interaction sites. The structure of the complex accounts for previous mutagenesis and structural observations and shows that the Fc forms a complementary crown across the convex surface of the receptor. Comparison of the complex with the isolated IgE-Fc crystal structure suggests that large structural changes may occur upon IgE binding to its receptor (see No. 60/189,403, ibid.) The IgE-Fc:FcεRIα complex provides a model for understanding the function of other antibody Fc-receptors and new conceptual approaches to the inhibition of IgE-mediated diseases.

[0121] B. Structure Determination of the Complex

[0122] The crystallization of the IgE-Fc:FcεRIα complex required the expression of each protein using recombinant baculovirus technology. The expression of the FcεRIα was carried out essentially as described previously¹¹. The IgE heavy chain contains four constant domains (Cε1-Cε4), in contrast to the three found in IgG antibodies. The interaction of FcεRI with IgE has been previously mapped to the two C-terminal constant domains of the IgE-Fc (domains Cε3/Cε4)¹²⁻¹⁶. The expression and purification of the human IgE-Fc Cε3/Cε4 domains was established as described (No. 60/189,403, ibid.) and purified protein used to form complexes with FcεRIα. The best complex crystals (spacegroup P42₁2) obtained with the wild type (wt) FcεRIα protein were small (˜60-100 μ/edge) and diffraction data was limited to a resolution of ˜4.5 Å (Table 3, crystal form I). In order to improve the complex crystals, a triple carbohydrate mutant of FcεRIα (FcεRIαΔ4-6) was expressed in insect cells. The FcεRIαΔ4-6 mutant lacks carbohydrate at three of the seven native attachment sites (residues 74, 134, 140) and was previously shown to produce ˜50% of the wt protein in CHO cells¹⁷. Complexes formed with baculovirus-expressed FcεRIαα4-6 grow crystals in spacegroup R32 and diffract X-rays to a resolution of 3.25 Å (Table 3, crystal form II). The structure was determined by molecular replacement techniques as described in Methods. Manual model building was done with the program O¹⁸ and refinement carried out with CNS¹⁹. Current refinement statistics for the complex are shown in Table 3, with an overall R-free of 29.3% and R-cryst of 27.0% to 3.25 Å. FIG. 1a shows electron density from a sigmaa-weighted 2Fo-Fc simulated annealing omit map calculated with the current model phases.

[0123] C. Overview of the Complex

[0124] Both crystal forms of the IgE-Fc:FcεRIα complex contain a single 1:1 complex in the asymmetric unit, with similar overall geometric features (FIGS. 1b, c). Given the low resolution of crystal form I, detailed interpretation of the interfaces is limited to crystal form II. Binding interactions are formed exclusively between the N-terminal Cε3 domains of the IgE-Fc with FcεRIα. The Cε4 domains of the IgE-Fc point away from the receptor structure and make no contacts with either receptor domain. The Cε3/Cε4 hinge regions are also not involved in direct receptor contacts. The two Cε3 domains are related by a nearly perfect diad axis (180.7° rotation), except for residues in the Cε2/Cε3-linker region (residues 331-336) (FIGS. 1b, c). The Cε4 domains are also related by a nearly perfect diad axis (179.6° rotation), but the orientation of this axis differs from that determined for the Cε3 domains (FIGS. 1b,c). The angle between the Cε3 and Cε4 domains also differs from that seen in the IgE-Fc alone (see 60/189,403, ibid.) While structured carbohydrate is visible in both the IgE-Fc and FcεRIα proteins, the carbohydrate groups do not contribute significantly to interactions between the two molecules. In addition, the IgE-Fc carbohydrate does not make any contacts across the IgE-Fc diad axis, but lies along the surface of each IgE-Fc domain.

[0125] The IgE-Cε3 domains bind at the top of the FcεRIα D1/D2 interface and along the backside of the D2 domain. The receptor contains two distinct binding sites for the two Cε3 domains. Site 1 refers to the interaction of one Cε3 domain exclusively with the C-C′ region of the receptor D2 domain, as indicated, while Site 2 refers to the interaction of the second Cε3 domain with the top of the receptor at the D1/D2 interface (FIG. 1b,c). Site 1 is centered around Y131 on the C′ loop in the receptor D2 domain. Site 2 is located at the top of the receptor and involves four surface-exposed tryptophans (W87, W110, W113, and W156). The two chains of the Fc molecule bind the receptors using surface loops in Cε3 that are distal to the Cε4 domains. These loops are the immunoglobulin-fold BC (362-364), DE (394-395), and FG (424-427) loops, in addition to residues in the Cε2/Cε3-linker region near the interchain disulfide (328-336). The linker regions between the Cε2 and Cε3 domains are involved in interactions with the FcεRIα, which cause both linker segments to point up and away from the complex interface. The role of the IgE-Fc Cε4 domains is to provide a structural dimerization scaffold that enables two Cε3 domains to form the bivalent interaction with FcεRIoα.

[0126] D. Structural Basis for the Formation of a 1:1 Complex

[0127] Biophysical studies of the IgE-Fc:FcαFRα complex in solution indicate that a 1:1 complex is formed between the antibody and FcεRI²⁰⁻²³. This contrasts with models with a 2:1 stoichiometry that have been proposed for the interaction of the IgG antibody with the FcγRIIa and FcγRIIb receptors²⁴⁻²⁶, as well as with the crystal structure of the MHC-class I like neonatal Fc receptor with IgG²⁷⁻²⁹. The observation of a 1:1 complex in both of the IgE-Fc:FcεRIα complex crystal forms is consistent with data on these complexes obtained using gel filtration and analytical ultracentrifugation techniques^(22,23). In principle, the 1:1 stoichiometry could arise due to FcεRI-induced conformational changes in the IgE-Fc, creating asymmetry in the Fc region, or by the binding of FcεRI across the Fc two-fold axis, creating a steric inhibition for the binding of a second receptor.

[0128]FIGS. 2a and 2 b show surface representations of the IgE-Fc:FcεRIα complex, demonstrating how the convex surface of the receptor interacts asymmetrically with the two IgE-Fc Cε3 domains. The receptor is positioned near the Fc-diad axis. There are two structural keys that dictate the formation of complexes with this stoichiometry: (1) The induction of structural asymmetry in the IgE-Fc Cε2/Cε3 linker and (2) Steric hindrance that blocks the binding of a second receptor.

[0129] Structural differences in the IgE-Fc domains are easily visualized by the superposition of the two Cε3 domains as shown in FIG. 2c. This superposition demonstrates that the Cε2/Cε3 linker regions comprised of residues 327-336, are constrained to an asymmetric arrangement by interactions with FcεRI. Other loops that are involved in distinct interactions with the two FcεRI binding sites also adopt slightly different conformations in the two Cε3 domains, such as the FG loops indicated in FIG. 2c.

[0130] Binding of one receptor to sites 1 and 2 creates a steric block of the binding of a second receptor. FIG. 2d shows representations of the both the IgE-Fc and FcεRIα in which the complex has been separated to exposed the buried interaction surfaces. The Cε2/Cε3 linker amino acids form the top of an arch that conforms to the convex surface of FcεRIα, generating an asymmetric binding site for a single receptor. While some of the Cε3 binding surface remains accessible to the interaction with a second receptor, superposition of a second receptor onto the 1:1 complex shows significant steric overlap between receptors and the IgE-Fc Cε2/Cε3 linker amino acids. Thus the binding of one receptor effectively prevents the binding of a second due to both the asymmetric arrangement of the IgE-Fc Cε2/Cε3 linker and by receptor binding across the Fc diad axis. Both contribute sterically to interfering with the binding of a second receptor. Although different residues in the Fc are used to form sites 1 and 2, there are four residues (R334, G335, V336, and H424) common to both sites, providing direct interactions that prevent the simultaneous binding of two receptors to one IgE-Fc.

[0131] E. Structural Changes in the Receptor and IgE Conformations upon Binding.

[0132] The receptor shows little change in conformation upon complex formation with the Fc. The overall RMS difference in 158 Cα positions compared to the unbound receptor¹¹ is 1.11 Å. There are two loops on the receptor which adopt different conformations from those seen in the original FcεRIα structure¹¹, the BC loop in D1 (residues 30-35) and the C′ strand in D2 (residues 127-133). The D2 C′ strand is longer in the FcεR1α:IgE-Fc complex compared to the FcεRIα structure alone. In the receptor structure, the C strand forms hydrogen bonds to the C′ strand through residue L127¹¹, while in the complex, the main chain hydrogen bonds extend to Y 131. However, analysis of the FcεRIα structure in multiple crystal forms (Garman et al., in preparation) shows that the C′ strand can adopt a variety of conformations depending on the chemical environment. The BC loop in Domain 1 also adopts different conformations in different crystal forms, but this region is not involved in IgE-Fc interactions.

[0133] The IgE-Fc in the complex is observed in a conformation that is very similar to the Fc domains of IgG antibodies^(30,31). Similar binding interactions between IgG antibodies and FcγRs could form an analogous 1:1 complex, as suggested by biophysical studies of the IgG-Fc interaction with FcγRIII³². In contrast to the similarities of the bound IgE-Fc to IgG-Fc structures, the crystal structure of the IgE-Fc alone shows a large re-arrangement of the two Cε3 domains that is greater than the conformational variation observed in IgG-Fc structures (see P_AL-9, ibid.). The IgE-Fc conformation may change substantially from the unbound conformation, which may exist in multiple conformational states that interact weakly with the receptor. This conformational variation in the IgE-Fc structure suggests new avenues to inhibiting IgE-receptor interactions using allosteric modulators that could stabilize the closed, unbound IgE-Fc structure.

[0134] F. Details of the Binding Surfaces of the FcR:IgE Interaction

[0135] The surface areas of both the IgE-Fc and FcεRIα that are involved in binding are shown in FIG. 2d, forming a total buried surface of ˜1890 Å². The IgE-Fc adopts a concave or crown-like configuration at the N-terminal ends of the two Cε3 domains that matches the convex shape of the receptor, with the top of the crown defined by the Cε2/Cε3 linker residues. The two Cε3 domains form two distinct sets of interactions with the receptor that involve an overlapping but non-identical set of IgE residues in each of these two sites. Of the fifteen FcεRI residues that contact the IgE-Fc, seven are aromatic and five of these aromatic residues are surface exposed tryptophans. In contrast, of the nineteen IgE-Fc residues that contact the FcεRIα, none are aromatic. The large fraction of aromatic receptor residues that are involved in this interaction and the large buried surface area may both contribute to the stability of the complex (K_(D)˜10⁻⁹-10⁻¹⁰ M).

[0136]FIG. 3a shows a plot of the IgE-Fc residues that are buried in the interaction with the receptor. Cε3 residues involved in Site 1 are in the top half of the plot and form specific interactions with FcεRIα residues shown in FIG. 3b. Nine amino acids from the IgE and seven amino acids from the receptor form Site 1 (FIG. 3b and FIG. 4a), burying a total of ˜835 Å² of surface area. The IgE residues are from four distinct regions of the IgE-Fc sequence that are predominantly loop and adjacent strand residues, including the N-terminal linker (residues 334-336), the BC loop (residues 362-364), the DE loop (residues 394-395) and the FG loop (residue 424). The receptor residues derive from two regions of the D2 domain, involving the C strand (residues 117 and 119) and the flexible C′-E region (residues 126 and 129-132). Two potential salt bridges (αK1 17-Cε3D362 and αE132-Cε3R334) and 4 potential hydrogen bonds (αK117-Cε3G335, αY129-Cε3D362, αY131-Cε3D364 and (αY131-Cε3H424) are formed across the Site 1 interface (FIG. 3b, FIG. 4a).

[0137] The Cε3 residues that are buried in the formation of Site 2 are shown in the bottom panel of FIG. 3a, FIG. 3c and in FIG. 4b. Residues R334, G335, V336, and H424 are buried in both Site 1 and Site 2 interfaces (FIG. 3a) but the remaining residues are unique to each of the two binding sites. Site 2 is larger than Site 1, with 10 amino acids from the IgE and 8 amino acids from the receptor forming a buried interface of 1040 Å². The IgE residues are localized to two distinct regions of the sequence, including extensive interactions with the Cε2/Cε3-linker region (residues 332-336) and the FG loop (residues 424-427). The FcεRIα residues are from three regions of the sequence (FIGS. 3c and 4 b), the D1D2 linker region (residues 85-87), the BC loop (residues 110 and 113) and the FG loop (residues 156-158). Residues from the receptor D1 domain do not form direct interactions with the IgE-Fc, but are likely important for stabilizing the conformation of the D1D2 linker residues, including the highly conserved W87 (FIGS. 3c and 4 b). In contrast to the Site 1 interface, Site 2 contains primarily hydrophobic amino-acids with limited polar interactions. Site 2 involves 3 potential hydrogen bonds across the interface (αW156-Cε3G335, αQ157-Cε3N332 and αQ157-Cα3R334). The large amount of buried hydrophobic surface area may contribute to the high affinity binding constant.

[0138] G. Electron density appears for CHAPS detergent molecules in the Form II crystals.

[0139] One of these molecules sits above FcεRI-W156 and below the Cε3-FG loop near H424 in Site 2 (FIG. 3d). The position of the CHAPS heterocyclic core is analogous to the position of the FcR C′ loop residues in Site 1. Although the CHAPS interaction may be weak, this structure provides a foundation for using combinatorial synthetic chemistry methods to improve these initial binding interactions^(33,34). A high affinity inhibitor of the Site 1 interactions could prove to be a viable inhibitor of the IgE binding, given mutagenesis data that indicate the importance of this site in overall IgE:FcεRI affinity. In addition, H424, which is located next to the CHAPS binding site, makes contacts with the receptor in both Site 1 and Site 2. A small molecule inhibitor that could interact with both the Y131 pocket of Cε3 (site 1) and with H424 might effectively disrupt both Site 1 and Site 2 interactions with the receptor.

[0140] H. Locations of IgE and FcR Mutations in the Structure of the Complex.

[0141] Mutagenesis studies of both the IgE-Fc and FcεRIα have been carried out in efforts to define the residues in both proteins that contribute to the stability of the complex. For FcεRIα, these studies have implicated residues located in the D2 domain, including amino acids 87, 113, 115, 117, 118, 120, 121, 122, 123, 128, 129, 130, 131, 132, 149, 153, 155, 156, 159, 160, 161^(11,35-39). While the general location of these residues is consistent with the observed complex, not all of the residues make direct contacts with the IgE-Fc, as shown in FIGS. 4a and 4 b. Of the residues identified by mutagenesis techniques, eight are observed to interact directly with the IgE (87, 113, 117, 129, 130, 131, 132, 156), twelve are within three residues that interact (115, 118, 120, 121, 122, 123, 128, 153, 155, 159, 160, 161) and the remaining amino acid (149) is buried and forms part of the hydrophobic core of D2.

[0142] The identification of the IgE-Fc binding site for receptor has implicated regions near the Cε2/Cε3 linker, the Cε3-AB helix and the Cε3-CD loop^(12,15,16,40,41). In general, most studies concur that the Cε2 and Cε4 domains do not interact directly with antibody. Residues in the IgE-Fc AB helix are likely to have an indirect effect on receptor binding, by altering the flexibility and geometry of the Cε3/Cε4 interface. Mutagenesis techniques have identified residues 333, 334, 376, 378, 380, 393, 414, 427 and 430 as possible contact residues in the IgE-Fc. Of these residues, three are observed as contact residues (333, 334, 427), one is within three residues (430) of a contact. However, four of these residues are located in the CD loop of Cε3 and are distant from the IgE-Fc:FcεRIα interface (376, 378, 380, 414). Not all mutations at these residues are deleterious, for example R376A or R376K has little effect on binding, while R376E reduces the binding to receptor. Similarly, D409A, D409E or D409N are well tolerated, while D409R disrupts receptor binding. Thus it is possible that these selective mutations have an indirect effect on receptor binding, potentially through alterations in the conformation of the Cε3 domain.

[0143] I. The basis for IgE Specificity and Implications for Other Receptor:Antibody Complexes

[0144]FIGS. 4a and 4 b show schematic diagrams of the amino acid residues that lie within 4 Å of each other in the Site 1 and Site 2 interfaces. Direct contacts are indicated by the connecting lines, which highlight residues that form the largest number of atomic contacts across the respective interfaces. Also shown are the residues that are found in the related human IgG receptors (FcγR1, FcγRII and FcγRIII, to the left) and in four subtypes of IgG antibodies (to the right).

[0145] In Site 1 there is little conservation of the residues that form the IgE-Fc:FcεRIα interface. Three residues are completely conserved (IgE residues 335, 362 and 394) in the Fc sequences, while there is poor conservation in the receptor sequences, except for the partial conservation of K117 and the relatively conserved Y129 (either Y or F). Interestingly, the conservation of K117 in three of the four receptors matches the complete conservation of D362 and G335, potentially preserving one of the two Site 1 salt bridges and one of the Site 1 hydrogen bonds. The conservative substitution of Y129 for F or Y in the IgG receptors also suggests that this site may be found in IgG-Fc complexes with the FcγRs. However, Y131, which forms a large number of atomic contacts across the interface and is buried in a shallow surface pocket on the IgE-Fc, is not conserved in the FcγRs (changing to either H or R). Given the central location of Y131 to the IgE interface, this residue may play an important role in immunoglobulin class specificity (FIG. 3b). For example, four of the five contact residues in IgE for Y131 are also different in the IgG-Fc sequences. In general, residues within the four IgG subtypes are highly conserved in the Site 1 interface (7/9 identical), as compared to the significant variation in the FcγR residues. FIG. 4b shows the conservation of interactions that are central to the Site 2 interface. P426 and L425 are absolutely conserved in all IgG Fc sequences and P426 interacts with two absolutely conserved tryptophans in the FcεR complex (W87 and W110). The two tryptophans form a hydrophobic pocket on the surface of the receptor into which the proline inserts (FIGS. 3c and 4 c). Site 2 also includes three residues (IgE residues 332-334) that have been shown to affect binding of IgG subtypes to FcγRI. IgG1 binds with high affinity to FcγRI, whereas IgG2 does not, and the difference in binding affinity can be introduced into IgG1 by the substitution of residues LLG to PVA (IgE residues 332-334, highlighted in black in FIG. 4b)⁴²,⁴³. This region of the IgE-Fc interacts with the FcεRIα FG loop residues 156-158 (FIGS. 3c and 4 b). Previous mutagenesis experiments have also shown that the transfer of the FcεRIα FG loop to FcγRII confers detectable IgE binding⁴⁴. Thus, residues involved in the formation of Site 2 are implicated in the binding and specificity of both IgE and IgG FcRs, consistent with a conserved binding mode across these members of the FcR family. Overall, five residues are completely conserved in these human receptors and IgG sequences that could form a common set of contacts. Variation in the FcγR FG loop sequences that contact the N-terminal linker region of the Fc fragment may provide key interactions that modulate the affinity of interaction of specific FcR:IgG pairs.

[0146] J. Conclusions

[0147] The crystal structure of the IgE-Fc:FcεRIα complex clarifies the atomic interactions that regulate the specificity and stoichiometry of protein:protein interactions underlying allergy and anaphylaxis. Similar complexes may form between IgG antibodes with their receptors, as suggested by previous mutagenesis studies and the structural analysis presented here, in contrast to models proposed for the interaction of IgG-Fc with the low affinity receptor, FcγRIIb²⁵ and FcγRIIa²⁴. Knowledge of these interactions may allow the development of inhibitors for the treatments of allergy and asthma and may also facilitate the targeted engineering of therapeutic antibodies to interact with specific subsets of the FcR family⁴⁵.

[0148] The observed flexibility in the IgE Cε3/Cε4 hinge (see 60/189,403, ibid.) and the distinct interactions of the two Cε3 domains in Site 1 and Site 2, are consistent with a kinetic scheme for IgE binding shown in FIG. 5. In this scheme, the independent binding of each Cε3 domain in the FcεRIα complex, leads to two pathways for the full dissociation of the complex. Surface plasmon resonance studies of IgE-Fc dissociation show two distinct kinetic dissociation rates that were hypothesized to represent the interaction of two different binding interactions between the IgE-Fc and FcεRIα, consistent with this kinetic scheme^(16,41). The IgE-Fc mutation R334S affects the biphasic dissociation kinetics of the IgE-Fc:FcεRIα complex by selectively accelerating the slow dissociation rate¹⁶. R334 is used in distinct and specific ways in Site 1 and Site 2, forming a salt bridge in Site 1 and van der Waals contacts in Site 2, consistent with the observation that one of these interactions could be more sensitive to the R334S mutation. The two dissociation pathways shown in FIG. 5 could exhibit two distinct overall kinetic rates that could be selectively affected by the R334S mutation. If the two Cε3 domains bind independently, with transient exposure of each site in the complex, inhibitors for either Site 1 or Site 2 could potentially accelerate the dissociation of receptor-bound IgE. Such inhibitors might prove useful in the treatment of acute allergic reactions in which dissociation of mast-cell associated IgE would be beneficial.

[0149] A model for the formation of a complex between an intact IgG antibody and Fc-receptor is shown in FIG. 6. In this model the crystal structure of the low affinity IgG receptor (FcγRIIb)²⁵ and one of the available intact IgG antibody structures (1IGY)⁴⁶ were superimposed on the IgE-Fc:FcεRIα complex. Superposition of the IgG structure is based on the Site 2 interactions, and this places the second IgG-Fc Cg2 domain within close proximity of the Site 1 binding surface without any conformational rearrangements (FIG. 6). The Fab arms of IgG are flexible and are also easily accommodated into this complex. Antigen-induced crosslinking of antibody:FcR complexes, leads to the co-localization of Fc receptors and the initiation of intracellular signal transduction cascades^(2,47). Within the one of the IgE-Fc:FcεRIα crystal forms and the IgE-Fc crystals (60/189,403, ibid.), Cε3 domains from adjacent molecules are observed to form packing interactions in the crystal through a strand to strand hydrogen-bonding interaction. Such interactions could potentially play a role in orienting crosslinked receptors, allowing the intracellular approach of receptor-associated kinases to adjacent γ-chain cytoplasmic tails, initiating the signal transduction cascade. A potential role for Cε3:Cε3 interactions in signal transduction remains to be tested.

[0150] K. Methods

[0151] 1. Crystallization of the Human IgE-Fc:FcεRIα Complex

[0152] Human IgE-Fc Cε3/Cε4 domains and a carbohydrate mutant of the FcεRIα¹¹ were expressed in insect cells essentially as described for IgE-Fc Cε3/Cε4 in 60/189,403. Complexes of wt-Fc-Cε3/Cε4 and wt-FcεRIα produced only poorly diffracting crystals. Since the receptor is heavily glycosylated (˜33% carbohydrate by weight), and the carbohydrate sites are dispersed on the receptor surface, a subset of these attachment sites was removed to improve the protein crystallization. A previously-described carbohydrate mutant of the receptor¹⁷ lacking three of the seven wild type carbohydrate sites (residues 74, 135, and 140) located on both D1 and D2 in the receptor structure. The triple receptor mutant, FcεRIαΔ4-6 was subcloned into the pvl1392 baculovirus transfer vector and recombinant virus produced. The mutant receptor was active, expressed well and was purified by affinity chromatography similarly to the wt protein. Purified wt-Fc and (αΔ4-6 or wt-α were incubated to form complex, which was subsequently purified by gel filtration chromatography using a Pharmacia Superdex 75 column and concentrated to 10 mgs/ml. Crystallizations were carried out using the the hanging drop method of vapor diffusion. Crystals of the wtIgE-Fc:wt-FcεRIα complex were grown from 1.4-1.6M Ammonium Sulfate, 100 mM Tris pH 8.5, over a period of 8-12 months (Form I). Purified wtIgE-Fc:αA4-6 complex was crystallized using 100 mM Tris, pH 8.5, 1.4-1.6M Ammonium Sulfate, and 8 mM CHAPS at room temperature. Crystals were then moved into harvest buffer (Form I: 2.1-2.7M Ammonium Sulfate, 100 mM Tris pH 8.5 or Form II: 1.6-2.0 M Ammonium Sulfate, 100 mM Tris pH 8.5, and 0.8 mM CHAPS). Crystals were frozen in harvest buffer supplemented with 15% glycerol. Data sets were collected at ALS 5.0.2 beamline and the APS DNDCAT 5-ID-B beamline at −160 C using an ADSC Quantum 4 detector or a MarCCD detector. Images were processed using the DENZO/SCALEPACK programs⁴⁸. Form I crystals belong to spacegroup P4₁ 2 ₁2 with cell dimensions a=b=126 Å, c=129 Å and Form II crystals belong to the space group R32 with cell dimensions a=192.8 Å and c=302.4 Å (hexagonal setting). Intensities were adjusted using the TRUNCATE program prior to molecular replacement using the AMoRe⁴⁹ and EPMR programs⁵⁰. 2. Crystal Structure Determination and Refinement

[0153] Molecular replacement for the Form II crystal was performed using coordinates from the 2.4 Å structure of the receptor¹¹. The use of normalized structure factors in AMoRe was critical to the success of the search. Both AMoRe and EPMR produced crystallographically equivalent locations for the receptor. 2Fo-Fc electron density maps with phases from the receptor revealed density corresponding to the two Cε3 portions of the Fc. A model for the core residues of Cε3 was created (see 60/189,403, ibid.) based upon homologous residues from an intact IgG structure 1IGT 46 A new 2Fo-Fc map was created with phases from the receptor and core residues of Cε3. This map showed density for the locations of the two Cε4 domains. A model for the core residues in Cε4 was made based upon the homologous residues in 1IGT. Rigid body refinement of the receptor, the core residues in Cε3, and the core residues in Cε4 reduced the Rfree to 45%. 2Fo-Fc maps and composite omit maps revealed clear density for protein and carbohydrate atoms absent from the model. The Form I crystal structure was solved by molecular replacement using the complex model from Form II, with a clear top solution. Given the limited resolution of Form I, refinement was limited to rigid body minimization.

[0154] Refinement was continued with the 3.25A Form II data using the CNS program¹⁹. Non-crystallographic symmetry restraints of 300 kcal/mol/A² were imposed on all atoms in the Fc except the loops that interact with the receptor. Refinement was performed using all data from 40-3.25 Å with |F|>0 and using a bulk solvent correction. After inserting all the missing loops from the protein chains, CHAPS molecules were located as large peaks of positive density in Fo-Fc maps. The current refinement statistics are summarized in TABLE 3 Figures were made using the programs Molscript⁵¹ and Grasp⁵². Data Collection and Refinement Statistics Data Data Set Form I Form II-Low Res. Form II-High Res. Resolution (Å)‡ 30-4.5 (4.66-4.5) 30.0-4.00 (4.14-4.00) 40.0-3.25 (3.37-3.25) Source APS DND 5ID ALS 5.02 APS DND 5ID Wavelength (Å) 1.0000 1.2000 1.0340 Completeness‡ 99.5 (97.7) 99.7 (98.3) 99.7 (98.7) Ave. Redundancy‡ 7.0 (5.8) 5.0 (3.9) 3.7 (3.4) Rmerge‡ 17.8 (57.5) 15.2 (75.0) 12.4 (90.1) I/sigI‡ 5.9 (2.0) 4.4 (2.0) 13.3 (1.5) observations (unique)‡ 39925 (5703) 91617 (18459) 125663 (34235) # refl in refinement (free) 18455 (945) 34156 (1736) Refinement (Form II, 3.25 Å) Rfactor/Rfree Total # atoms Protein Carbohydrate Detergent Sulfate 25.8/28.1 5251 4821 259 146 25 RMSD Average B Bonds Angles Overall Receptor Fc chain 1 Fc chain 2 0.0102 1.58 91.0 63.2 94.9 99.4 Ramachandran Favored Allowed Generous Disallowed 77.0% 21.5% 1.5% 0.0%

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[0207] While the various embodiments of the present invention have been described in detail, it is apparent that modifications and adaptations of those embodiments will occur to those skilled in the art. It is to be expressly understood, however, that such modifications are adaptations are within the scope of the present invention, as set forth in the following claims.

1 6 1 528 DNA Homo sapiens CDS (1)..(528) 1 gtc cct cag aaa cct aag gtc tcc ttg aac cct cca tgg aat aga ata 48 Val Pro Gln Lys Pro Lys Val Ser Leu Asn Pro Pro Trp Asn Arg Ile 1 5 10 15 ttt aaa gga gag aat gtg act ctt aca tgt aat ggg aac aat ttc ttt 96 Phe Lys Gly Glu Asn Val Thr Leu Thr Cys Asn Gly Asn Asn Phe Phe 20 25 30 gaa gtc agt tcc acc aaa tgg ttc cac aat ggc agc ctt tca gaa gag 144 Glu Val Ser Ser Thr Lys Trp Phe His Asn Gly Ser Leu Ser Glu Glu 35 40 45 aca aat tca agt ttg aat att gtg aat gcc aaa ttt gaa gac agt gga 192 Thr Asn Ser Ser Leu Asn Ile Val Asn Ala Lys Phe Glu Asp Ser Gly 50 55 60 gaa tac aaa tgt cag cac caa caa gtt aat gag agt gaa cct gtg tac 240 Glu Tyr Lys Cys Gln His Gln Gln Val Asn Glu Ser Glu Pro Val Tyr 65 70 75 80 ctg gaa gtc ttc agt gac tgg ctg ctc ctt cag gcc tct gct gag gtg 288 Leu Glu Val Phe Ser Asp Trp Leu Leu Leu Gln Ala Ser Ala Glu Val 85 90 95 gtg atg gag ggc cag ccc ctc ttc ctc agg tgc cat ggt tgg agg aac 336 Val Met Glu Gly Gln Pro Leu Phe Leu Arg Cys His Gly Trp Arg Asn 100 105 110 tgg gat gtg tac aag gtg atc tat tat aag gat ggt gaa gct ctc aag 384 Trp Asp Val Tyr Lys Val Ile Tyr Tyr Lys Asp Gly Glu Ala Leu Lys 115 120 125 tac tgg tat gag aac cac aac atc tcc att aca aat gcc aca gtt gaa 432 Tyr Trp Tyr Glu Asn His Asn Ile Ser Ile Thr Asn Ala Thr Val Glu 130 135 140 gac agt gga acc tac tac tgt acg ggc aaa gtg tgg cag ctg gac tat 480 Asp Ser Gly Thr Tyr Tyr Cys Thr Gly Lys Val Trp Gln Leu Asp Tyr 145 150 155 160 gag tct gag ccc ctc aac att act gta ata aaa gct ccg cgt gag aag 528 Glu Ser Glu Pro Leu Asn Ile Thr Val Ile Lys Ala Pro Arg Glu Lys 165 170 175 2 176 PRT Homo sapiens 2 Val Pro Gln Lys Pro Lys Val Ser Leu Asn Pro Pro Trp Asn Arg Ile 1 5 10 15 Phe Lys Gly Glu Asn Val Thr Leu Thr Cys Asn Gly Asn Asn Phe Phe 20 25 30 Glu Val Ser Ser Thr Lys Trp Phe His Asn Gly Ser Leu Ser Glu Glu 35 40 45 Thr Asn Ser Ser Leu Asn Ile Val Asn Ala Lys Phe Glu Asp Ser Gly 50 55 60 Glu Tyr Lys Cys Gln His Gln Gln Val Asn Glu Ser Glu Pro Val Tyr 65 70 75 80 Leu Glu Val Phe Ser Asp Trp Leu Leu Leu Gln Ala Ser Ala Glu Val 85 90 95 Val Met Glu Gly Gln Pro Leu Phe Leu Arg Cys His Gly Trp Arg Asn 100 105 110 Trp Asp Val Tyr Lys Val Ile Tyr Tyr Lys Asp Gly Glu Ala Leu Lys 115 120 125 Tyr Trp Tyr Glu Asn His Asn Ile Ser Ile Thr Asn Ala Thr Val Glu 130 135 140 Asp Ser Gly Thr Tyr Tyr Cys Thr Gly Lys Val Trp Gln Leu Asp Tyr 145 150 155 160 Glu Ser Glu Pro Leu Asn Ile Thr Val Ile Lys Ala Pro Arg Glu Lys 165 170 175 3 528 DNA Homo sapiens CDS (1)..(528) 3 gtc cct cag aaa cct aag gtc tcc ttg aac cct cca tgg aat aga ata 48 Val Pro Gln Lys Pro Lys Val Ser Leu Asn Pro Pro Trp Asn Arg Ile 1 5 10 15 ttt aaa gga gag aat gtg act ctt aca tgt aat ggg aac aat ttc ttt 96 Phe Lys Gly Glu Asn Val Thr Leu Thr Cys Asn Gly Asn Asn Phe Phe 20 25 30 gaa gtc agt tcc acc aaa tgg ttc cac aat ggc agc ctt tca gaa gag 144 Glu Val Ser Ser Thr Lys Trp Phe His Asn Gly Ser Leu Ser Glu Glu 35 40 45 aca aat tca agt ttg aat att gtg aat gcc aaa ttt gaa gac agt gga 192 Thr Asn Ser Ser Leu Asn Ile Val Asn Ala Lys Phe Glu Asp Ser Gly 50 55 60 gaa tac aaa tgt cag cac caa caa gtt gct gag agt gaa cct gtg tac 240 Glu Tyr Lys Cys Gln His Gln Gln Val Ala Glu Ser Glu Pro Val Tyr 65 70 75 80 ctg gaa gtc ttc agt gac tgg ctg ctc ctt cag gcc tct gct gag gtg 288 Leu Glu Val Phe Ser Asp Trp Leu Leu Leu Gln Ala Ser Ala Glu Val 85 90 95 gtg atg gag ggc cag ccc ctc ttc ctc agg tgc cat ggt tgg agg aac 336 Val Met Glu Gly Gln Pro Leu Phe Leu Arg Cys His Gly Trp Arg Asn 100 105 110 tgg gat gtg tac aag gtg atc tat tat aag gat ggt gaa gct ctc aag 384 Trp Asp Val Tyr Lys Val Ile Tyr Tyr Lys Asp Gly Glu Ala Leu Lys 115 120 125 tat tgg tat gag aac cac gct atc tcc att aca aat gcc gca gct gaa 432 Tyr Trp Tyr Glu Asn His Ala Ile Ser Ile Thr Asn Ala Ala Ala Glu 130 135 140 gac agt gga acc tac tac tgt acg ggc aaa gtg tgg cag ctg gac tat 480 Asp Ser Gly Thr Tyr Tyr Cys Thr Gly Lys Val Trp Gln Leu Asp Tyr 145 150 155 160 gag tct gag ccc ctc aac att act gta ata aaa gct ccg cgt gag aag 528 Glu Ser Glu Pro Leu Asn Ile Thr Val Ile Lys Ala Pro Arg Glu Lys 165 170 175 4 176 PRT Homo sapiens 4 Val Pro Gln Lys Pro Lys Val Ser Leu Asn Pro Pro Trp Asn Arg Ile 1 5 10 15 Phe Lys Gly Glu Asn Val Thr Leu Thr Cys Asn Gly Asn Asn Phe Phe 20 25 30 Glu Val Ser Ser Thr Lys Trp Phe His Asn Gly Ser Leu Ser Glu Glu 35 40 45 Thr Asn Ser Ser Leu Asn Ile Val Asn Ala Lys Phe Glu Asp Ser Gly 50 55 60 Glu Tyr Lys Cys Gln His Gln Gln Val Ala Glu Ser Glu Pro Val Tyr 65 70 75 80 Leu Glu Val Phe Ser Asp Trp Leu Leu Leu Gln Ala Ser Ala Glu Val 85 90 95 Val Met Glu Gly Gln Pro Leu Phe Leu Arg Cys His Gly Trp Arg Asn 100 105 110 Trp Asp Val Tyr Lys Val Ile Tyr Tyr Lys Asp Gly Glu Ala Leu Lys 115 120 125 Tyr Trp Tyr Glu Asn His Ala Ile Ser Ile Thr Asn Ala Ala Ala Glu 130 135 140 Asp Ser Gly Thr Tyr Tyr Cys Thr Gly Lys Val Trp Gln Leu Asp Tyr 145 150 155 160 Glu Ser Glu Pro Leu Asn Ile Thr Val Ile Lys Ala Pro Arg Glu Lys 165 170 175 5 669 DNA Homo sapiens CDS (1)..(666) 5 gcg gat ccc tgt gat tcc aac ccg aga ggg gtg agc gcc tac cta agc 48 Ala Asp Pro Cys Asp Ser Asn Pro Arg Gly Val Ser Ala Tyr Leu Ser 1 5 10 15 cgg ccc agc ccg ttc gac ctg ttc atc cgc aag tcg ccc acg atc acc 96 Arg Pro Ser Pro Phe Asp Leu Phe Ile Arg Lys Ser Pro Thr Ile Thr 20 25 30 tgt ctg gtg gtg gac ctg gca ccc agc aag ggg acc gtg aac ctg acc 144 Cys Leu Val Val Asp Leu Ala Pro Ser Lys Gly Thr Val Asn Leu Thr 35 40 45 tgg tcc cgg gcc agt ggg aag cct gtg aac cac tcc acc aga aag gag 192 Trp Ser Arg Ala Ser Gly Lys Pro Val Asn His Ser Thr Arg Lys Glu 50 55 60 gag aag cag cgc aat ggc acg tta acc gtc acg tcc acc ctg ccg gtg 240 Glu Lys Gln Arg Asn Gly Thr Leu Thr Val Thr Ser Thr Leu Pro Val 65 70 75 80 ggc acc cga gac tgg atc gag ggg gag acc tac cag tgc agg gtg acc 288 Gly Thr Arg Asp Trp Ile Glu Gly Glu Thr Tyr Gln Cys Arg Val Thr 85 90 95 cac ccc cac ctg ccc agg gcc ctc atg cgg tcc acg acc aag acc agc 336 His Pro His Leu Pro Arg Ala Leu Met Arg Ser Thr Thr Lys Thr Ser 100 105 110 ggc ccg cgt gct gcc ccg gaa gtc tat gcg ttt gcg acg ccg gag tgg 384 Gly Pro Arg Ala Ala Pro Glu Val Tyr Ala Phe Ala Thr Pro Glu Trp 115 120 125 ccg ggg agc cgg gac aag cgc acc ctc gcc tgc ctg atc cag aac ttc 432 Pro Gly Ser Arg Asp Lys Arg Thr Leu Ala Cys Leu Ile Gln Asn Phe 130 135 140 atg cct gag gac atc tcg gtg cag tgg ctg cac aac gag gtg cag ctc 480 Met Pro Glu Asp Ile Ser Val Gln Trp Leu His Asn Glu Val Gln Leu 145 150 155 160 ccg gac gcc cgg cac agc acg acg cag ccc cgc aag acc aag ggc tcc 528 Pro Asp Ala Arg His Ser Thr Thr Gln Pro Arg Lys Thr Lys Gly Ser 165 170 175 ggc ttc ttc gtc ttc agc cgc ctg gag gtg acc agg gcc gaa tgg gag 576 Gly Phe Phe Val Phe Ser Arg Leu Glu Val Thr Arg Ala Glu Trp Glu 180 185 190 cag aaa gat gag ttc atc tgc cgt gca gtc cat gag gca gcg agc ccc 624 Gln Lys Asp Glu Phe Ile Cys Arg Ala Val His Glu Ala Ala Ser Pro 195 200 205 tca cag acc gtc cag cga gcg gtg tct gta aat ccc ggt aaa tga 669 Ser Gln Thr Val Gln Arg Ala Val Ser Val Asn Pro Gly Lys 210 215 220 6 222 PRT Homo sapiens 6 Ala Asp Pro Cys Asp Ser Asn Pro Arg Gly Val Ser Ala Tyr Leu Ser 1 5 10 15 Arg Pro Ser Pro Phe Asp Leu Phe Ile Arg Lys Ser Pro Thr Ile Thr 20 25 30 Cys Leu Val Val Asp Leu Ala Pro Ser Lys Gly Thr Val Asn Leu Thr 35 40 45 Trp Ser Arg Ala Ser Gly Lys Pro Val Asn His Ser Thr Arg Lys Glu 50 55 60 Glu Lys Gln Arg Asn Gly Thr Leu Thr Val Thr Ser Thr Leu Pro Val 65 70 75 80 Gly Thr Arg Asp Trp Ile Glu Gly Glu Thr Tyr Gln Cys Arg Val Thr 85 90 95 His Pro His Leu Pro Arg Ala Leu Met Arg Ser Thr Thr Lys Thr Ser 100 105 110 Gly Pro Arg Ala Ala Pro Glu Val Tyr Ala Phe Ala Thr Pro Glu Trp 115 120 125 Pro Gly Ser Arg Asp Lys Arg Thr Leu Ala Cys Leu Ile Gln Asn Phe 130 135 140 Met Pro Glu Asp Ile Ser Val Gln Trp Leu His Asn Glu Val Gln Leu 145 150 155 160 Pro Asp Ala Arg His Ser Thr Thr Gln Pro Arg Lys Thr Lys Gly Ser 165 170 175 Gly Phe Phe Val Phe Ser Arg Leu Glu Val Thr Arg Ala Glu Trp Glu 180 185 190 Gln Lys Asp Glu Phe Ile Cys Arg Ala Val His Glu Ala Ala Ser Pro 195 200 205 Ser Gln Thr Val Gln Arg Ala Val Ser Val Asn Pro Gly Lys 210 215 220 

What is claimed is:
 1. A three-dimensional model selected from the group consisting of: (a) a three-dimensional model of a complex between (i) an extracellular domain of a human high affinity Fc epsilon receptor alpha chain (FcεRIα) protein and (ii) a human IgE Fc region comprising Cε3 and Cε4 domains (Fc-Cε3/Cε4), wherein said model substantially represents the atomic coordinates specified in Table 1; and (b) a three-dimensional model comprising a modification of said model of (a), wherein said modification represents a complex between a Fc receptor protein that binds to a Fc domain of an antibody and an antibody Fc region that binds to a Fc receptor protein the hinge between domain Cε3 and domain Cε4 of the Fc-Cε3/Cε4 region, and a FcεRIα:Fc-Cε3/Cε4 region that interacts with 3-[3-(cholamidopropyl) dimethylammonio]-1-propane-sulfonate (CHAPS).
 2. A method to produce the three-dimensional model of claim 1, wherein the three-dimensional model is the complex between the extracellular domain of a human FcεRIα protein and a human Fc-Cε3/Cε4 region, said method comprising representing amino acids of said protein and said region in said complex at substantially the atomic coordinates specified in Table
 1. 3. A method to produce the three-dimensional model of a complex between (i) an extracellular antibody binding domain of an antibody receptor protein other than human FcεRIα as represented by coordinates in Table 1 and (ii) an antibody receptor binding domain of an antibody other than human IgE as represented by coordinates in Table 1, said method comprising homology modeling.
 4. An isolated crystal of a complex between an extracellular domain of a FcεRIα protein and an IgE Fc-Cε3/Cε4 region.
 5. A method to produce the isolated crystal of claim 4, wherein the complex is between an extracellular domain of a FcεRIα protein and an IgE Fc-Cε3/Cε4 region, said method comprising vapor diffusion.
 6. A method to identify a compound that inhibits the binding between an IgE antibody and a FcεRIα protein, said method comprising using a three-dimensional model of a complex between an extracellular domain of a human high affinity FcεRIα protein and a human Fc-Cε3/Cε4 region to identify said compound, wherein said model substantially represents the atomic coordinates specified in Table
 1. 7. An inhibitory compound identified in accordance with the method of claim
 6. 8. A therapeutic composition comprising an inhibitory compound of claim
 7. 9. A method to protect an animal from allergy, said method comprising administering to said animal an inhibitory compound of claim
 7. 10. A compound that inhibits the binding between an IgE antibody and a FcεRIα protein, said compound identified by analysis of a three-dimensional model of a complex between an extracellular domain of a human high affinity FcεRIα protein and a human Fc-Cε3/Cε4 region to identify said compound, wherein said model substantially represents the atomic coordinates specified in Table
 1. 11. A polypeptide selected from the group consisting of a FcεRIα:Fc-Cε3/Cε4 interaction site 1, a FcεRIα:Fc-Cε3/Cε4 interaction site 2, a C strand of domain 2 of FcεRIα, a C′E loop of domain 2 of FcεRIα, a tryptophan-containing hydrophobic ridge of FcεRIα, a crystal contact cluster involved in IgE binding; a FG loop in D2; a D1D2 interface; a cleft between D1 and D2; a domain 1; a domain 2; a hydrophobic core; a A′B loop of D1; a EF loop of D1; a BC loop of D2; a CC′ loop of D2; and a strand of D2.
 12. An isolated nucleic acid molecule encoding the polypeptide of claim
 11. 13. A method of using the three-dimensional model of claim 1, comprising: (a) analyzing the three-dimensional model substantially representing the atomic coordinates specified in Table 1 to identify at least one amino acid of a target protein represented by said three-dimensional model which if replaced by said identified amino acid(s) to improve a function of said target protein; and (b) replacing said identified amino acid(s) to produce a mutein having at least one of said improved function.
 14. The method of claim 13, wherein said target protein is a Fc-Cε3/Cε4 protein, a FcεRIα protein or a protein comprising SEQ.ID NO.2, and wherein said improved function is selected from the group comprising: (a) increased stability, increased affinity for an IgE binding domain of a FcεRIα protein, altered substrate specificity or increased solubility when said target protein is the Fc-Cε3/Cε4 protein; and (b) increased stability, increased affinity for an Fc-domain of an antibody, altered substrate specificity or increased stability when said target protein is the FcεRIα protein or the protein comprising SEQ.ID NO.2.
 15. A mutein produced by the method of claim 14, wherein said mutein has at least one improved function compared to the target protein, wherein said target protein is the FcεRIα protein, the Fc-Cε3/Cε4 protein or the protein comprising SEQ.ID NO.2.
 16. The mutein of claim 15 having an improved function compared to an unmodified FcεRIα protein, wherein the amino acid sequence of said mutein differs in at least one position from the amino acid sequence of said unmodified protein, said position being in a region selected from the group consisting of a crystal contact cluster, a tryptophan-containing hydrophobic ridge, a FG loop in D2, a D1 D2 interface, a cleft between D1 and D2, a domain 1, a domain 2, a hydrophobic core, a A′B loop of D1, a EF loop of D1, a BC loop of D2, a C strand of D2, a CC′ loop of D2, a C′E loop of D2, a strand of D2, the amino terminal five residues of said protein, and the carboxyl terminal five residues of said protein.
 17. An isolated nucleic acid sequence encoding a mutein of claim
 15. 18. A recombinant virus comprising said nucleic acid sequence of claim
 17. 19. A recombinant cell comprising said nucleic acid sequence of claim 17, wherein said cell is capable of expressing said nucleic acid sequence.
 20. A diagnostic reagent comprising a mutein of claim
 15. 21. A therapeutic composition comprising a mutein of claim
 15. 22. A method to use a mutein of claim 15, wherein said method is selected from the group consisting of: (a) a method to protect an animal from allergy, said method comprising administering a therapeutic composition comprising said mutein to said animal; (b) a method to detect allergy, or susceptibility thereto, in an animal, said method comprising using said mutein to detect said allergy; and (c) a method to enhance the performance of an IgE binding assay, said method comprising incorporating into said assay said mutein. 